NLK-NML/MeSH-CZ-2025-notes huggingface dataset:
hemoglobin Bonn: causes falsely decreased oxygen saturation measurements in pulse oximetry; mutation: his to asp at position 87 in alpha globin chain
hemoglobin Boras: leu replaced by arg at position alpha2beta2(88)(f4)
hemoglobin Boyle Heights: asp deleted at position 6(a4) on alpha chain
hemoglobin Brem-sur-Mer: serine at position 9 of the beta-chain is replaced by tyrosine
hemoglobin Brent: asparagine replaces histidine at position 117(g19) of the beta subunit
hemoglobin Brest: glutamine replaced by lysine on beta chain at position 127(h5)
hemoglobin Brie Comte Robert: a hemoglobin variant with high oxygen affinity and marked hydrophobic properties
hemoglobin Brisbane: produces mild erythrocytosis; high oxygen affinity; leu replaced by his at position 68(e12) on beta chain
hemoglobin British Columbia: glu replaced by lys on alpha 2 beta 2(101) chains
hemoglobin Brockton: ala replaced by pro at beta138(h16); associated with mild anemia
hemoglobin Bronovo: his replaced by leu at alpha2 103 position, associated with alpha thalassemia phenotype
hemoglobin Bronte: glycine replaces valine at position 93(fg5) of the alpha-chain
hemoglobin Broussais: asn replaces lys at position alpha 92(fg2)
hemoglobin Brugg: has alpha1-globin mutation (alpha20(b1)his to gln
hemoglobin Bruxelles: results from deletion of one of the two adjacent phenylalanines, beta41 or beta42 (alpha2abeta241 or 42(c7 or dc1))
hemoglobin Buenos Aires: phe replaced by ser at position 85(f1) on beta chain
hemoglobin Buffalo: glutamine replaces histidine at position 89(fg1) of the alpha1 chain
hemoglobin Bunbury: asp replaced by asn at position 94(fg1) on beta chain
hemoglobin Burgos: mutation: alpha1 cd64(e13)(asp->asn): a hemoglobin variant detected during follow-up of diabetic patients
hemoglobin Bushey: leucine replaces phenylalanine at position 122(gh5) of beta chain
hemoglobin Bushwick: glycine replaced by valine in position beta 74(e18)
hemoglobin Buzen: threonine replaces alanine at position 138(h16) of the beta chain
hemoglobin C Ziguinchor: causes hereditary persistence of fetal hemoglobin; glutamic acid replaced by valine & proline replaced by arginine
hemoglobin C-Harlem: mutant hemoglobin; glutamic acid replaced by valine at position 6 on beta chain & aspartic acid replaced by asparagine at position 73 on beta chain
hemoglobin Caen: val replaced by gly at alpha132(h15) position
hemoglobin Calais: ala replaced by pro at position beta76(e20); hemoglobin variant with decreased intrinsic oxygen affinity
hemoglobin Cambridge-MA: a high oxygen affinity variant that has a mutation in exon 3 of beta chain at position 144 resulting in replacement of a lysine residue by a stop codon (beta144, aag>tag, hgvs:hbb c.433 a>t)
hemoglobin Camden: gln replaced by glu at position 131(h9) on beta chain
hemoglobin Camperdown: arg replaced by ser at position alpha2 beta2 104 (g6)
hemoglobin Campinas: valine replaces alanine at position 26(b7) of alpha chain
hemoglobin Canebiere: lysine replaces asparagine at position 102(g4) of the beta chain
hemoglobin Canterbury: phenylalanine replaces cysteine at position 122(g14) of the beta subunit
hemoglobin Capa: aspartic acid replaced by glycine(beta2) at position 94 of alpha2(g1) chain
hemoglobin Cardarelli: an unstable and hyperaffine variant in association with beta(+)-thalassemiahas with mutation (beta86(f2)ala to pro)
hemoglobin Caruaru: serine replaces phenylalanine at position 122(gh5) of the beta chain
hemoglobin Casablanca: methionine and leucine replace lysine and phenylalanine at positions 65(e9) and 122(gh5), respectively, on the beta chain
hemoglobin Caserta: threonine replaces alanine at position 26 of the alpha chain
hemoglobin Castilla: mutation localized in the heme pocket; leu replaced by arg at position 32(b14) on beta chain
hemoglobin Catonsville: glu inserted between pro-37(c2)alpha & thr-38(c3alpha)
hemoglobin Cemenelum: arg replaced by trp at position alpha92(fg4)
hemoglobin Chad: glu replaced by lys at position 23(b4) on alpha chain
hemoglobin Chandigarh: asp replaced by gly at alpha2beta2-94(fg1)
hemoglobin Chapel Hill: asp replaced by gly at position alpha(2)74(ef3); associated with beta-thalassemia
hemoglobin Charolles: tyrosine replaces histidine at position 103 of the g10 chain of the alpha1 subunit
hemoglobin Chartres: an unstable alpha2-globin variant with phe to ser substitution at alpha33(b14)
hemoglobin Chesapeake: arg replaced by leu at position 92(fe4) on alpha chain
hemoglobin Chesterfield: arg replaes beta28leu; produces phenotype of inclusion body beta-thalassemia
hemoglobin Cheverly: phe replaced by ser at position 45(cd4) on beta chain
hemoglobin Chiapas: pro replaced by arg at position 114 on alpha chain
hemoglobin Chicago: leu replaced by met at position 136 of alpha chain; do not confuse with hb north chicago
hemoglobin Chico: lysine replaced by threonine at position 66(e10) on beta chain
hemoglobin Chile: methionine replaces leucine at position 28(b10) of the beta subunit
hemoglobin Chongqing: leu replaced by arg at position alpha2(na2)
hemoglobin Christchurch: phe replaced by ser at position 71 of beta chain
hemoglobin City of Hope: gly replaced by ser at position 69 of beta chain
hemoglobin Cleveland: has two amino substitutions; glu substituted by gln at beta 121(gh4) position & cys substituted by arg at alpha(2)beta(2)93(f9) position
hemoglobin Clinico-Madrid: arginine replaces lysine at position 90(fg2) of the alpha chain
hemoglobin Cocody: asp replaced by asn at position 21(b3) on beta chain
hemoglobin Coimbra: high oxygen affinity variant; asp is replaced by glu at codon 99 of the beta chain
hemoglobin Collingwood: unstable hb variant; val replaced by ala at position 60(e4) on beta chain
hemoglobin Columbia Missouri: alpha2(88(f9)ala---val)beta2; high oxygen affinity hemoglobin that causes erythrocytosis
hemoglobin Complutense: gln replaced with glu at position alpha2 beta2 127(h5)
hemoglobin Connecticut: low oxygen affinity; asp replaced by gly at position 21(b3) on beta chain
hemoglobin Contaldo: ser replaced by arg at position 103(g10) on alpha chain
hemoglobin Cook: a hemoglobin variant with lysine replaced by threonine in position beta 132(h10)
hemoglobin Cordele: asp replaced by ala at position 47 of the alpha chain
hemoglobin Costa Rica: beta 77(ef1) his-->arg - result of a somatic cell mutation at codon 77 of the beta gene
hemoglobin Cowtown: his replaced by leu at position 146 on beta chain
hemoglobin Crete: substitution: beta129(h7)ala to pro
hemoglobin Creteil: ser replaced by asn at position 89 on beta chain
hemoglobin Cubujuqui: arg replaced by ser at position 141 on alpha chain
hemoglobin D: gly replaced by asp at position 15 on alpha chain; hb dab & hb db are phenotypes
hemoglobin D Granada: glutamic acid replaced by valine at position 22(b4) of the alpha2beta2 chain
hemoglobin D Ibadan: (beta87)thr replaced by lys; initially reported in a man from ibadan, nigeria
hemoglobin D Iran: abnormality on beta chain; do not confuse with hemoglobin sickle d iran
hemoglobin D Ouled Rabah: asn is replaced by lys at position beta19(b1)
hemoglobin D-Agri: has (beta9(a6)ser replaced by tyr & beta121(gh4)glu replaced by gln; an east indian hemoglobin variant with two amino acid substitutions
hemoglobin D-Neath: alanine replaces glutamic acid at position 121(gh4) on beta chain
hemoglobin Dagestan: lys replaced by glu at position 60(e9) on alpha chain; found in dagestan ussr
hemoglobin Dallas: an alpha-chain variant with a substitution of lys for asn at position 97(g4)
hemoglobin Daneshgah-Tehran: his replaced by arg beta(2) at position alpha(2) 72(ef1)
hemoglobin Daphne: human mutant hemoglobin synthesized in e coli as cleavable fusion protein; cys-93 beta replaced by ser, his-143 beta replaced by arg
hemoglobin Davenport: asn replaced by his at position 78(ef7) on the alpha(2) chain
hemoglobin Debrousse: beta96(fg3) leu replaced by pro
hemoglobin Decines-Charpieu: threonine replaces alanine at position 69(e18) of the alpha subunit
hemoglobin Deer Lodge: his is replaced by arg in position 2 of beta chain
hemoglobin Delfzicht: lysine replaces asparagine at position 9(a7) of the alpha chain
hemoglobin Denver: phe replaced by ser at position alpha(2)beta(2)41(c7)
hemoglobin Dhofar: pro replaced by arg in position 58 of the beta chain
hemoglobin Dhonburi: val replaced by gly at position alpha2beta2 126(h4); unstable beta variant producting a beta-thalassemia intermedia phenotype in association with b(0)-thalassemia
hemoglobin Die: alanine replaces valine at position 93(fg5) of alpha subunit
hemoglobin Djelfa: unstable beta chain variant; val replaced by ala at alpha2beta(2)98(fg5)
hemoglobin Doha: val substituted by glu at position 1 of beta chain; present in 3 members of a qatari family
hemoglobin Dongguan: homozygous mutation in exon 2 of the alpha1-globin gene (alpha52(e1)ser->cys (tct>tgt); hba1: c.158c>g)
hemoglobin Douala: alpha3(a1)ser replaced by phe; an alpha1 gene mutation in a cameroonian woman heterozygous for hb s and a 3.7 kb deletional alpha-thalassemia
hemoglobin Duan: asp replaced by ala at position 75(ef4) on alpha chain; found in china
hemoglobin Duino: this new variant contains both the mutations of hb newcastle and that of hb camperdown
hemoglobin Dunn: asp replaced by asn at position 6(a4) on the alpha chain
hemoglobin E Saskatoon: glutamic acid replaced by lysine at position alpha2 beta2 22(b4)
hemoglobin East Timor: mutation: beta80(ef4)asn replaced by his
hemoglobin Einstein: a semisynthetic hemoglobin in which residues 23-26 are deleted from the alpha-chain
hemoglobin El Escorial: aspartic acid replaces valine at position 96(g3) of the alpha chain
hemoglobin Ethiopia: alpha chain slow-moving variant; tyr replaced by his at position alpha(2)140(hc2)
hemoglobin Etobicoke: ser replaced by arg at position 84(f5) on the alpha chain; also listed as alpha 85(f5)
hemoglobin Evans: unstable hemogloin causing a midl hemolytic anemia; val replaced by met at position 62(e11) on the alpha2 chain
hemoglobin Evanston: trp replaced by arg at position 14(a12) on alpha chain
hemoglobin Extremadura: val replaced by leu at alpha2beta2133(h11)
hemoglobin F Austell: arg replaced by lys at position alpha2ggamma2 40(c6)
hemoglobin F Baskent: ala replaced by thr at position alpha(2)agamma128(h6)
hemoglobin F Bonaire-Ga: glutamine replaced by arginine at position 39(c5) on the a(gamma) chain
hemoglobin F Brooklyn: lys replaced by glu at position 66(e10) on the alpha(2)-g(gamma)2 chain
hemoglobin F Calabria: leucine replaces phenylalanine at position 118(gh1) of the g(gamma) subunit
hemoglobin F Calluna: thr replaced by arg at position 12(a9) of alpha chain
hemoglobin F Caltech: lys replaced by gln at position 120(gh 3) on g(gamma) chain; four gamma chains present in above hemoglobin
hemoglobin F Campinas: glutamine replaces glutamic acid at g121(gh4) of agamma chain
hemoglobin F Catalonia: a ggamma chain variant in which tryptophan is replaced by arginine at position gamma15(a12) chain
hemoglobin F Charlotte: ile replaced by thr at position 75 and ala replaced by gly at position 136; both on gamma chain
hemoglobin F Chori-I: aspartic acid replaces glycine at position 16(a13) of the gamma-chain
hemoglobin F Chori-II: glutamic acid replaces glycine at position 29(b11) on the gamma-chain
hemoglobin F Clamart: asparagine replaces lysine at position 17(a14) of the gamma chain
hemoglobin F Columbus-Ga: asp replaced by asn at position 94 on g(gamma) chain
hemoglobin F Forest Park: ile replaced by thr at 75(e19) & asp replaced by asn at 73(e17) on the gamma globin chain
hemoglobin F Fukuyama: asp replaced by asn on a(gamma)t43(cd2) position
hemoglobin F Granada: asp replaced by val at position alpha2ggamma2 22(b4)
hemoglobin F Hayward: aspartic acid replaces glycine at position 1 of gamma-chain
hemoglobin F Iwata: gly replaced by arg at position 72(e16) on gamma chain; found in japan
hemoglobin F Jiangsu: val replaced by met at position 134(h12) of the a(gamma) chain
hemoglobin F Joanopolis: alanine replaces aspartic acid at position 73(e17) of ggamma chain
hemoglobin F Kennestone: his replaced by arg at position 77 on gamma chain
hemoglobin F Kingston: met replaced by arg at position 55(d6) on gamma chain
hemoglobin F Kotobuki: glu replaced by gly at position 6 on gamma chain
hemoglobin F La Grange: glu replaced by lys at position 101(g3) on gamma chain
hemoglobin F Lesvos: ile replaced by thr at position 75(e19) on alpha2ggamma2
hemoglobin F Lodz: ser replaced by arg at position 44 on gamma chain
hemoglobin F M Osaka: his replaced by tyr at position alpha2ggamma2(63)(e7)
hemoglobin F Malta I: his replaced by arg at position alpha2(g)gamma2 117(g19)
hemoglobin F Meinohama: fetal hb variant; gly replaced by gln at position 5(a2) on gamma chain; abnormal gamma chain has ile at position 75 & gly at position 136
hemoglobin F Onoda: his replaced by tyr at the 146(hc3) position on the alpha(2)-g(gamma)2 chain
hemoglobin F Osilo: serine replaces glycine at position 119(gh2) of the agamma chain
hemoglobin F Ouled Rabah: lysine replaces asparagine at position 19(b1) of the gamma chain
hemoglobin F Paulinia: tyrosine replaces aspartic acid at position 80(ef4) of ggamma chain
hemoglobin F Pordenone: glu replaced by gln at position 6(a3) on gamma chain; ile at position 75(a3) & ala at position 136(a3) on gamma chain
hemoglobin F Sardinia: ile replaced by thr at position 75 on a(gamma) chain
hemoglobin F Seattle: abnormal fetal hemoglobin; contains 3 base substitution mutations; do not confuse with hemoglobin seattle
hemoglobin F Siena: glu replaced by lys at position 121 on alpha(2)a(gamma)t(2) chain
hemoglobin F Texas: glutamic acid replaced by lysine at position 5 or 6 on the gamma chain
hemoglobin F Xin-Su: aspartic acid replaced by histidine at position i73(e17) on a(gamma) chain
hemoglobin F Xingjiang: glycine replaced by arginine at position t25(b7) on a(gamma) chain
hemoglobin F Yamaguchi: asp replaced by asn at position 80(ef4) on gamma chain
hemoglobin F-Albaicin: lys replaced by glu or gln at position 8(5a) on the gamma chain
hemoglobin F-Auckland: asp replaced by asn at gamma 7(a4)
hemoglobin F-Beech Island: ala replaced by asp at position gamma 53
hemoglobin F-Bron: alanine replaces valine at position 20(b2) of the gamma chain
hemoglobin F-Brugine Feldkirch: histidine replaces leucine at position 105(g7) of the gamma chain
hemoglobin F-Cincinnati: phe replaced by ser at position alpha(2)(g)gamma(2)41(c7)
hemoglobin F-Clarke: lys replaced by asn at position alpha2(ggamma2)(65)(e9)
hemoglobin F-Cobb: trp replaced by gly at position 37(c3) of gamma chain
hemoglobin F-Coignieres: valine replaces isoleucine at position 75(e19) of the gamma chain
hemoglobin F-Cosenza: fast-moving gamma chain variant in which gly is replaced by glu at position 25 of g(gamma) chain
hemoglobin F-Dammam: asp replaced by asn at position alpha2agamma2(79)(ef3)
hemoglobin F-Emirates: lysine replaced by glutamic acid at position 59(e3) of g-gamma chain
hemoglobin F-Macedonia-I: alpha2(a)gamma2(2)(na2)-his replaced by gln
hemoglobin F-Macedonia-II: asparagine replaces lysine at position 104(g6) on ggamma chain
hemoglobin F-Oakland: glu replaced by lys at position alpha2(ggamma)i2(26(b8)
hemoglobin F-Pendergrass: pro replaces arg at position gamma36(c2)
hemoglobin F-Porto Torres: substitutions: agamma75(e19)ile to thr & 136(h14)ala to ser; variant of the agamma chain having two substitutions, one being that of hb f-sardinia
hemoglobin F-Sacromonte: glutamine replaces lysine at position 59(e3) on the g(gamma2) chain
hemoglobin F-Saskatoon: glu replaced by lys at position alpha(2)(g)gamma(2)21(b3)
hemoglobin F-Sassari: ile replaced by thr at position (g)gamma 75; also has gly at position 136
hemoglobin F-Tokyo: val replaces ile at position alpha2ggamma2 34(b16)
hemoglobin F-Urumqi: asp residue replaced by gly at position 22 of the gamma chain
hemoglobin F-Veleta: arg replaced by gly at position alpha2(g)gamma2 40(c6)
hemoglobin FM Fort Ripley: tyr replaced by his at position 92 alpha2gamma2; causes cyanosis in newborns; analogous to the beta-chain adult hemoglobin mutant: hemoglobin m hyde park
hemoglobin Fannin-Lubbock: gly replaced by asp at position 119(gh2) of normal hemoglobin consisting of 2 alpha & 2 beta chains
hemoglobin Fontainebleau: ala replaced by pro at alpha21(b2)
hemoglobin Fort Worth: alpha chain variant; glu replaced by gly at position alpha2(27)(b8)beta2
hemoglobin Frauenfeld: phenylalanine replaces serine at position 138(h21) of the alpha-chain
hemoglobin Fuchu-I: his replaced by tyr of alpha chain at position 72(ef1)
hemoglobin Fuchu-II: asn replaced by his of alpha chain at position 97(g4)
hemoglobin Fukui: hemoglobin variant with (alpha139(hc1)lys to asn (aaa to aac) (alpha2))
hemoglobin Fukuoka: his replaced by tyr at the 2(na2) position on the beta chain
hemoglobin Fukutomi: abnormal hemoblobin in which aspartic acid is replaced by valine on alpha126(h9) chain; has high oxygen affinity
hemoglobin Fukuyama: his replaced by tyr at position beta77(ef1)
hemoglobin Fulton-Georgia: mutation: alpha 20(b1)his to pro
hemoglobin G Copenhagen: asp replaced by asn at position 47(cd6) on beta chain
hemoglobin G Coushatta: glu replaced by ala at position 22 on beta chain
hemoglobin G Ferrara: causes clinical symptoms similar to that of drepanocytic anemia; lysine replaces asparagine at position 57(e1) of the beta-chain; substitution located on residual portion of the molecule surface thus favoring hbs polymerization
hemoglobin G Georgia: pro replaced by leu at position alpha2 95 beta2
hemoglobin G Pest: asp replaced by asn at position 74(ef3) on alpha z chain
hemoglobin G Philadelphia: asn replaced by lys in position 68 on alpha chain
hemoglobin G San Jose: gly replaced by glu at position 7(a4) on beta chain
hemoglobin G Waimanalo: asp replaced by asn at position 64 on alpha chain
hemoglobin G-Makassar: alanine replaces glutamate at position 6(a3) of the beta chain
hemoglobin G-Szuhu: asparagine replaced by lysine at position beta 80
hemoglobin G-Taipei: glu replaced by gly at position 22(b4) of normal hemoglobin consisting of 2 alpha & 2 beta chains
hemoglobin Gainesville-Ga: beta chain variant; gly replaced by arg at position alpha2beta2(46)(cd5)
hemoglobin Galicia: unstable beta chain variant; his & val at position 97 & 98 are replaced by one leu residue; causes severe hemolytic anemia
hemoglobin Gambara: lysine replaced by glutamate at position 82 of the beta ef6 chain
hemoglobin Geelong: asn replaced by asp at postion beta139(h17)
hemoglobin Geneva: change in codon 114 from ctg(leu) to -gg that results in a frameshift and the presumed synthesis of an abnormal beta chain that is 156 residues long with a completely different c-terminal amino acid sequence
hemoglobin Genova: leu replaced by pro at position 28 on beta chain
hemoglobin Gerland: alanine replaces valine at position 55(e4) of the alpha2 chain
hemoglobin Godavari: pro replaced by thr at alpha95(g2) position
hemoglobin Gouda: an alpha chain variant with his replaced by gln at alpha72(ef1)
hemoglobin Grady: extended alpha chains due to repetitive insertion of 3 amino acids between positions 118 & 119
hemoglobin Graz: his replaced by leu at position 2 of the beta chain; found in four healthy unrelated adults
hemoglobin Grey Lynn: unstable hemoglobin; substitution (alpha91leu phe) affects heme interactions and alpha1beta2 contacts
hemoglobin Groene Hart: serine replaces proline at position 119 of the alpha1 chain
hemoglobin Guangzhou: asp repalced by gly at position alpha64(e13)
hemoglobin GuiZhou: pro replaced by arg at position alpha(2)77(ef6)
hemoglobin Görwihl: has the mutation (alpha2beta(2)5(a2)pro to ala), an electrophoretically silent variant with impaired glycation
hemoglobin Haaglanden: a nonsickling hemoglobin in which valine replaces glutamic acid at position 7 of the beta-chain
hemoglobin Hafnia: his replaced by gln at position alpha2(beta116(g18))
hemoglobin Hagerstown: alanine replaces proline at position 44(ce2) of the alpha1 chain
hemoglobin Hagley Park: has (alpha82ala-->thr) substitution; identified in an infant with severe hemolytic anemia
hemoglobin Hakkari: leucine replaced by arginine at position b13 on alpha2,beta2 chains
hemoglobin Hamadan: gly replaced by arg at position alpha 2 beta 2 56(d7)
hemoglobin Hamilton: val replaced by ile at position 11(a8) on beta chain
hemoglobin Hammersmith: mutant hemoglobin; phe replaced by ser at position 42 on beta chain
hemoglobin Hanamaki: lys replaced by glu at position 139 of the alpha chain
hemoglobin Handsworth: gly replaced by arg at position 18(a16) on alpha chain
hemoglobin Harbin: lys replaced by met at position alpha16 (a14)
hemoglobin Harrow: a neutral hemoglobin variant; phe replaced by cys at beta 118(gh1)
hemoglobin Hazebrouck: thr replaced by pro at position 38 on beta chain
hemoglobin Hb Ahvaz: mutation: alpha83(f4)leu to arg
hemoglobin Hb S-São Paulo: hbb:c.20a t p.glu6val; c.196a g p.lys65glu; a double-mutant hemoglobin in heterozygosis 18-month-old brazilian male with moderate anemia
hemoglobin Heathrow: phe replaced by leu at position beta103(g5)
hemoglobin Hekinan: glc replaced by asp at position alpha27(b8)
hemoglobin Henan: glutamine replaces glutamic acid at position 90(f6) of the beta chain
hemoglobin Henri Mondor: glu replaced by val at position alpha2 beta2 26(b8)
hemoglobin Heraklion: deletion of ccc between codons 36 and 37; results in loss of a proline residue
hemoglobin Hershey: glycine replaces alanine at position 70(e14) of the beta chain
hemoglobin Higashitochigi: results from the deletion of one of two glycines, beta24(b6) or beta25(b7); stays as an oxidized form; causes overt cyanosis but with little hemolysis
hemoglobin Hikari: lys replaced by asn at position 61(e5) on beta chain
hemoglobin Hillingdon: valine replaces phenylalanine at position 46(ce4) of the alpha chain
hemoglobin Himeji: ala replaced by asp at position betal40 (h18)
hemoglobin Hinsdale: asn replaced by lys at beta139(h17)
hemoglobin Hinwil: a beta chain variant with thr replaced by asn at beta38(c4)
hemoglobin Hirosaki: leucine replaces phenylalanine at position 43(ce1) of the alpha chain
hemoglobin Hirose: trp replaced by ser at position 37(c3) on beta chain
hemoglobin Hobart: his replaced by arg in position 20(b1) on alpha chain
hemoglobin Hofu: val replaced by glu at position 126 on beta chain
hemoglobin Hokusetsu: glycine replaces aspartic acid at position 52 of d3 beta chain
hemoglobin Hope: gly replaced by asp at position 136(h14) on beta chain
hemoglobin Hornchurch: lysine replaces glutamate at position 43(cd2) of the beta-chain
hemoglobin Hoshida: electrophoretically slow-moving hemoglobin variant; glu is replaced by gln at position 43(cd2) of the beta chain
hemoglobin Hotel-Dieu: asp replaced by gly at position 99 on beta chain
hemoglobin Howick: trp replaced by gly at position beta(37)(c3)
hemoglobin Hradec Kralove: alpha2beta2-115(g17)ala replaced by asp
hemoglobin I High Wycombe: lys replaced by glu at position beta59 (e3)
hemoglobin I Philadelphia: lys replaced by glu at position 16 on the alpha chain
hemoglobin I-Interlaken: gly replaced by asp at position 15(a13) of the alpha chain
hemoglobin II, Calyptogena: from the deep-sea clam, calyptogena kaikoi; amino acid
hemoglobin III, Lucina pectinata: consists of 152 amino acid residues, mw 18.068 kda including heme; aa sequence given in first source; from symbiont-harboring clam
hemoglobin IV: from glycera dibranchiata erythrocytes; amino acid sequence given in first source
hemoglobin Iberia: arginine replaces cysteine at position 104(g11) of the alpha-chain
hemoglobin Icaria: alpha chain variant with an elongation of 31 amino acid residues at the carboxy terminus & a taa-aaa mutation at codon 142; causes hb h disease
hemoglobin Ilmenau: cystine replaces phenylalanine at position 41(c7) of the beta chain
hemoglobin Indianapolis: produces phenotype of beta-thalassemia; leu replaced by arg at position 106 of the beta-globin chain
hemoglobin Inkster: valine replaces aspartic acid at position 85(f6) of the alpha chain
hemoglobin J Anatolia: lys replaced by thr at position 61(e10) of the alpha chain
hemoglobin J Antakya: lysine replaced with methionine at position alpha2 beta2 65(e9)
hemoglobin J Auckland: glycine replaced by aspartic acid at position 25(b7) on beta chain
hemoglobin J Baltimore: glycine replaced by aspartic acid at position 16(a13)
hemoglobin J Bangkok: glycine replaced by aspartic acid at position 56(d7) on beta chain
hemoglobin J Biskra: has deletion of eight residues, which included the distal histidine and its neighbours (alpha50-57, alpha51-58 or alpha52-59)
hemoglobin J Calabria: abnormal hemoglobin found in japanese family; gly replaced by asp at beta64(e8)
hemoglobin J Cape Town: arginine replaced by glutamine at position 92(fg4) on alpha chain
hemoglobin J Cordoba: lys replaced by met at position alpha(2)(a)beta(2)95(fg2)
hemoglobin J Daloa: asparagine replaced by aspartic acid at position 57(e1) on beta chain
hemoglobin J Guantanamo: alanine replaced by aspartic acid at position alpha2beta2 128(h6)
hemoglobin J Habana: alanine replaced by glutamic acid at position 71(e20) on alpha chain
hemoglobin J Iran: aspartic acid replaces histidine in position 77 of beta chain
hemoglobin J Jackson: lysine replaced by asparagine at position 127 on alpha chain
hemoglobin J Lens: alanine replaced by aspartic acid at position 13 on beta chain
hemoglobin J Lome: lysine replaced by asparagine at position 59(e3) on beta chain
hemoglobin J Meerut: abnormal hemoglobin found in japanese family; ala replaced by glu at alpha120(h3)
hemoglobin J Mexico: abnormal hemoglobin; gln replaced by glu at position 54 of the alpha chain
hemoglobin J Pointoise: alanine replaced by aspartic acid at position alpha2 63(e12) beta2
hemoglobin J Providence: lysine replaced by asparagine or aspartic acid at position alpha(2) beta(2) 82 (ef6)
hemoglobin J Rovigo: alanine replaced by aspartic acid(beta2) at alpha(2)53(e2) position
hemoglobin J Taichung: ala is replaced by asp at codon 129 of beta-chain
hemoglobin J Tongariki: alpha chain variant; affected chromosome carries only a single active alpha globin gene; this condition is present in alpha thalassaemia
hemoglobin J-Amiens: lys replaced by asn at beta17(a14); found in a japanese
hemoglobin J-Buda: asparagine replaces lysine at position 61(e10) of the alpha subunit
hemoglobin J-Camaguey: arginine replaced by glycine at position alpha 141(hc3)
hemoglobin J-Chicago: ala replaced by asp at beta76(e20) position; do not confuse with hb chicago/d-chicago/north chicago
hemoglobin J-Europa: ala replaced by asp at position beta62(e6)
hemoglobin J-Paris: alanine at position 12 of alpha chains is replaced by aspartic acid
hemoglobin J-Tashikuergan: alanine replaced by glutamic acid at position alpha(2)19(ab1)
hemoglobin Jacksonville: val replaced by asp at position alpha2beta2(54)(d5)
hemoglobin Jambol: hyperunstable hemoglobin that causes severe hemolytic anemia; has mutation that leads to a deletion of 4 amino acid residues (leu-leu-glu-asn) at positions 105-108 and an insertion of 9 residues (val-pro-ser-val-thr-leu-phe-phe-asp) at the same location, creating an abnormal elongated beta-chain of 151 amino acid residues
hemoglobin Jianghua: lys replaced by ile at position 120(gh3) on beta chain
hemoglobin Johnstown: silent variant; val replaced by leu at position 109(g11) on the beta chain
hemoglobin K Ibadan: (cd5)gly replaced by glu at position 46 on beta chain
hemoglobin K Woolwich: lys replaced by gln at position 132 on beta chain
hemoglobin Kalavasos: histidine replaces leucine at position 91(fg3) of the alpha-chain
hemoglobin Kanagawa: lys replaced by met at position alpha40(c5); shows increased oxygen affinity, decreased heme-heme interaction & lowered 2,3-diphosphoglycerate effect relative to normal
hemoglobin Kansas: mutation: beta102(g4)asn tothr, aac to acc
hemoglobin Karachi: ala replaced by pro at position 5 on alpha chain
hemoglobin Kariya: hb variant with increased oxygen affinity; lys replaced by glu in position alpha 40 (c5) at the alpha 1 beta 2 contact
hemoglobin Karlskoga: histidine replaces asparagine at position 21(b3) of the beta chain
hemoglobin Kempsey: asp replaced by asn at position 99 on beta chain
hemoglobin Kenitra: gly replaces arg at position alpha2 beta2 69(e13); associated with alpha-thalassemia
hemoglobin Kenya: a hybrid consisting of agamma (1-80) and beta (87-146); ggamma-globulin hereditary persistance of fetal hemoglobin
hemoglobin Khartoum: arginine replaces proline at position 124(h2) of the beta subunit
hemoglobin Knossos: ala replaced by ser in position 27 of beta chain; present as silent beta-thalassemia
hemoglobin Kochi: leucine at position 141 of the beta chain is replaced by valine and codon for lysine of position 144 replaced with stop codon
hemoglobin Kodaira: his replaced by gln at position beta146(hc3); hb kodaira ii results from a different base substitution (cag as opposed to caa in hb kodaira i)
hemoglobin Koelliker: found in patients suffering from favism; c-terminal 141-arg removed from alpha chain
hemoglobin Kofu: thr replaced by ile at position 84 on beta chain
hemoglobin Kokura: asp replaced by gly at position 47 on alpha chain
hemoglobin Koriyama: abnormal hemoglobin; tandem insertion of a five-residue segment which included the proximal histidine at beta92(f8)
hemoglobin Korle: aspartic acid replaced by asparagine at position 73 on beta chain
hemoglobin Koya Dora: results from an a-c mutation in the termination codon of alpha1 chain
hemoglobin Kurdistan: aspartic acid replaced by tyrosine at position 47 of alpha(ce5) chain
hemoglobin Kurosaki: lysine replaced by glutamic acid at position 7(a5) of alpha chain
hemoglobin L: minor hemoglobin isolated from haemolysates of chicken embryos
hemoglobin L'Aquila: a thalassemic hemoglobin variant with beta106(g8)leu-->val, ctg-->gtg mutation
hemoglobin La Desirade: unstable hemoglobin variant in which ala is replaced by val at position 129(h7) on the beta chain
hemoglobin La Pommeraie: valine replaces methionine at position 133(h11) of beta chain in a sicilian subject
hemoglobin La Roche-sur-Yon: partial amino acid sequence given in first source; an unstable variant with replacement of leu at position beta81 by his; has 2 variants (i & ii); variant ii has an additional deamination of asn at position beta80; rn given refers to hb la roche-sur-yon variant i
hemoglobin Las Palmas: mildly unstable hemoglobin variant; ser replaced by phe at position beta 49(cd8)
hemoglobin Le Lamentin: his replaced by gln at alpha 20(b1)
hemoglobin Leeds: has beta56(d7)gly-->cys mutation that aggravates anemia in a child with beta(0)-thalassemia trait
hemoglobin Legnano: arg replaced by leu at position 141 on alpha chain
hemoglobin Leiden: glu residue is deleted from position 6 or 7 of the beta chain
hemoglobin Lepore Baltimore: cross over between amino acid 50 of delta chain and amino acid 86 of beta chain; more recent data suggests the crossover occurs at leucine at position 68 of the delta chain and threonine at position 84 of the beta chain
hemoglobin Lepore Boston: amino acid 87 is delta globin & amino acid 116 is beta globin position; see also record for hemoglobin lepore baltimore
hemoglobin Lepore Boston-Washington: crossover occurs between glutamine at position 87 of delta chain and histidine at position 116 of beta chain; found in patient with beta-thalessemia; associated with unusual high level of hb f
hemoglobin Lepore-ARUP: corresponds to hb-lepore with a breakpoint between delta31leu and beta51thr
hemoglobin Lepore-Hollandia: cross over between amino acid 22 of delta chain and amino acid 50 of beta chain - (delta 1-22/beta 50-146)
hemoglobin Les Andelys: leu replaced by pro at alpha83(f4) position
hemoglobin Leu: synthetic hb; glu replaced by leu at position 6 on the beta chain by site-directed mutagenesis; used to study structure-function of sickle cell hemoglobin
hemoglobin Lille: asp replaced by ala at position 74(ef3) on alpha chain
hemoglobin Limassol: asparagine replaces lysine at position 8(a5) of the beta chain
hemoglobin Linkoeping: thr substituted for pro at position beta36 in c-helix
hemoglobin Lisbon: asparagine replaces glutamic acid at position 23(b4) of alpha chain
hemoglobin Louisville: leu replaced by phe at position 42 of the beta chain (cd1)
hemoglobin Loves Park: leu replaced by phe at beta68 (e12)
hemoglobin Lucknow: beta chain structural variant; shows clinical manifestations of beta-thalassemia
hemoglobin Lufkin: gly replaced by asp at position beta29(b11)
hemoglobin Lusaka: phenylalanine replaces serine at position 131(h14) of the alpha1 chain
hemoglobin Luton: his replaced by leu on alpha 89; polycythemia & microcytosis arising from a combination of this hemoglobin and an alpha thalassemia trait
hemoglobin Lyon-Bron: alpha 2 globin chain variant with low oxygen affinity affecting the n-terminal residue and leading to n-acetylation (alpha 1(na1)val replaced by ala); found in two members of a family of german ascent presenting with a moderate normocytic anemia
hemoglobin M Iwate: histidine replaced by tyrosine at position 87(f8) on alpha chain; also replaced by arginine
hemoglobin M(Ratnagiri): tyrosine replaces histidine at position 63 on the beta-chain
hemoglobin M101: high molecular weight extracellular hemoglobin extracted from arenicola marina
hemoglobin Machida: gln replaces glu at position 6 in beta chain
hemoglobin Madrid: proline replaces alanine at position 115(g17) of the beta chain
hemoglobin Madrid 2: a structural hemoglobin variant of (g)gamma with two amino acid replacements in cis found in the umbilical cord blood of a neonate in madrid, spain; two new mutations in cis on (g)gamma chain of fetal hemoglobin: (g gamma 50(d1)ser to cys) and (g gamma 75(e19)ile to thr); hb f-madrid is also available with a different mutation
hemoglobin Manitoba: his replaced by arg at position 102(g9) on alpha chain
hemoglobin Mantes-La-Jolie: ala replaced by thr at alpha79(ef8) position
hemoglobin Manukau: val replaced by gly at beta67(e11) position
hemoglobin Maputo: asp replaced by tyr at position 47(cd6) on beta chain; found in combination with hemoglobin s in child from mozambique
hemoglobin Marineo: valine replaces alanine at position 70(e14) of the beta-chain
hemoglobin Marseille: met residue extends the nh2 terminus; his replaces pro in position n2 on beta chain
hemoglobin Masuda: contains 2 substitutions in the beta chain; leu replaced by met at position beta114(g16) & gly replaced by asp at position beta119(gh2)
hemoglobin Matsue-Oki: aspartic acid replaced by asparagine at position 75 on alpha chain
hemoglobin Medicine Lake: beta32(b14) leu replaced by gln & 98(fg5) val replaced by met
hemoglobin Melusine: pro replaced by ser at alpha114(gh2) position
hemoglobin Miami: proline replaces histidine at position 116(g18) of the beta chain
hemoglobin Midnapore: valine replaces alanine at positiion 53(d4) of the beta-chain
hemoglobin Minneapolis-Laos: phe replaced by tyr at position 118 on beta chain
hemoglobin Mississippi: ser replaced by cys (or arg) on beta chain at position 44
hemoglobin Mito: lys replaced by glu at position beta 144(hc 1) with increased oxygen affinity
hemoglobin Miyada: abnormal globin chain possesses part of beta-chain & part of delta-chain; n terminal beta-globin sequence to amino acid 12 & c terminal delta-globin sequence from amino acid 22; anti-lepore hemoglobin
hemoglobin Miyano: thr replaced by ser at position alpha41(c6); high affinity alpha chain variant
hemoglobin Miyashiro: val replaced by gly at position 23 on beta chain
hemoglobin Mizuho: leu replaced by pro at position 68(e12) of the beta chain
hemoglobin Molfetta: leucine replaces valine at position 126(h4) of the beta subunit
hemoglobin Monroe: arg replaced by thr at position 30 on beta chain; variant associated with beta-thalassemia
hemoglobin Mont Saint Aignan: ala is replaced by pro at beta128(h6) position; an unstable variant leading to chronic microcytic anemia
hemoglobin Montefiore: tyrosine replaces aspartic acid at position 126(h9) of alpha chain
hemoglobin Montfermeil: beta 130(h8) tyr replaced by cys
hemoglobin Montreal: extended beta chain due to deletion of asp, gly, leu at positions 73,74, & 75 & an insertion of ala, arg, cys, gln at the same location
hemoglobin Moriguchi: his replaced by tyr at position 97(fg4) of the beta chain
hemoglobin Mosella: ala replaced by thr at alpha111(g18) position
hemoglobin Mozhaisk: his replaced by arg at position 92(f8) on beta chain
hemoglobin Mulhacen: ala replaced by ser at position alpha2 123(h6)
hemoglobin Munakata: lys is replaced by met at position fg2(90) on alpha chain
hemoglobin Muscat: leu replaced by val at beta32; a new variant in association with hb s in an arabian family
hemoglobin Muskegon: arg replaces gly at beta83(ef7) chain
hemoglobin NYU: asn replaced by lys at position 12 on delta chain
hemoglobin Nagasaki: beta17(a14)lys replaced by glu
hemoglobin Nantes: leucine replaces valine at position 34(b16) of the beta chain
hemoglobin Natal: alpha(2)(minus tyr-arg)beta(2); has high affinity for oxygen without a bohr effect & heme-heme interaction
hemoglobin Nedlands: valine replaces alanine at position 28(b9) of the alpha chain
hemoglobin Nevers: tyr replaced by ser alpha2beta2 130(h8)
hemoglobin New Mexico: associated with erythrocytosis; pro replaced by arg at position 100(g2) on beta chain
hemoglobin New York: val replaced by glu at position 113(g15) on beta chain
hemoglobin Nijkerk: tyrosine replaces alanyl-asparagine at positions 138 and 139 on beta subunit
hemoglobin Nikaia: aspartic acid replaces histidine at position 20(b1) of the alpha chain
hemoglobin Nikosia: lys replaced by gln at beta17(a14)
hemoglobin Nishinomiya: has (leu-gly-inserted between codons 69(e13) and 70(e14) of beta); an unstable hemoglobin with reduced oxygen affinity found in a patient with spherocytic hemolysis
hemoglobin Noah Mehmet Oeztuerk: tyrosine replaces histidine at position 143(h21) of the delta chain
hemoglobin North Chicago: high oxygen affinity hemoglobin variant; pro replaced by ser at position beta36 (c2)
hemoglobin North Shore: unstable hemoglobin; val replaced by glu at position beta 134
hemoglobin Nottingham: val replaced by gly at alpha(2)beta(2)98(fg5) position; causes severe hemolytic anemia
hemoglobin Nouakchott: pro replaced by leu at position alpha114(gh2)
hemoglobin Nunobiki: found in japanese male with marginal erthrocytosis; arg replaced by cys at the carboxy terminus of the alpha chain at position 141
hemoglobin Nympheas: human mutant hemoglobin synthesized in e coli as cleavable fusion protein; cys-93 beta replaced by ser
hemoglobin O Indonesia: (gh4)glu replaced by lys at position 116 on the alpha chain; rn given refers to cpd with unknown mf
hemoglobin O Padova: glu replaced by lys on alpha chain at position b11; association with osler-rendu disease
hemoglobin O-Tibesti: lysine replaces glutamate at position 121(gh4) and isoleucine replaces valine at position 11(a8) on the beta subunit; basically a combination of both hb o-arab and hb hamilton
hemoglobin Oegstgeest: serine replaces cysteine at position 104(g11) of the alpha1 chain
hemoglobin Oita: proline replaces histidine at position 45 of ce3 alpha chain
hemoglobin Okayama: alpha2beta2 2(na2) his replaced by gln
hemoglobin Okazaki: has (b93 (f8) cys to arg) mutation, a rare hemoglobin variant found in a family from naples, italy
hemoglobin Old Dominion Burton-upon-Trent: tyrosine replaces histidine at position 143(h21) of beta chain
hemoglobin Oleander: gln replaces glu acid in position 116 of alpha chain
hemoglobin Olinda: 22rd through 25th residues omitted from the beta-chain
hemoglobin Olmsted: an unstable hemoglobin with leu replaced by arg at position beta141 (h19)
hemoglobin Olomouc: ala replaced by asp at alpha2beta2(86)(f2)
hemoglobin Osler: tyr replaced by asp at position 145 on beta chain
hemoglobin Osu-Christiansborg: asparagine replaces aspartic acid at position 52(d3) of beta subunit
hemoglobin Owari: val replaced by met at position alpha121 (h 4)
hemoglobin Ozieri: val substituted for ala at position 71 of the alpha-globin chain
hemoglobin P-Galveston: arginine replaces histidine at position 117(g19) of the beta chain
hemoglobin P-Nilotic: formed by hybridization of beta chain with delta chain
hemoglobin Pakse: has taa to tat mutation at the terminating codon (codon 142) of the alpha2-globin gene
hemoglobin Palmerston North: val replaced by phe at position 23(b5) on beta chain
hemoglobin Papanui: arginine replaces lysine at position 99(g8) of the alpha-chain
hemoglobin Part-Dieu: threonine replaces alanine at position 65(e14) of alpha subunit
hemoglobin Pasadena: leu replaced by arg at position 75(e19) on beta chain
hemoglobin Passy: serine at position 81 of alpha-chain replaced by proline
hemoglobin Pavie: val replaced by glu at position alpha135(h18); interfers with measurement of glycated hemoglobin
hemoglobin Perpignan: serine replaces glycine at position 136(h14) of the beta chain
hemoglobin Perth-Abraham Lincoln: leu replaced by pro at position beta2(b14)
hemoglobin Peterborough: val replaced by phe at beta111(g13) position
hemoglobin Philly: tyr replaced by phe at position 35(c1) of normal hemoglobin consisting of 2 alpha chains and 2 beta chains
hemoglobin Phnom Penh: contains (alpha117phe(h1)-ile-alpha118thr(h2)); has insertion of residues in the third exon of the alpha1-globin gene
hemoglobin Pierre-Benite: glu replaced by asp at position beta 90(f6)
hemoglobin Pitie Salpetriere: val replaced by phe at position 34(b16) on beta chain
hemoglobin Plasencia: mutation: alpha125(h8)leu replaced by arg (alpha2); variant with an unstable alpha chain, associated with dyserythropoietic anemia
hemoglobin Poissy: gly replaced by arg at 56(d7) & ala replaced by pro at 86(f2) on the beta chain
hemoglobin Poitiers: histidine replaced by aspartic acid at position 45 of the alpha(ce3) chain
hemoglobin Port Huron: lysine replaced by arginine at position 56(e5) on alpha chain; abnormal peptide adjacent to the alpha t-6 peptide
hemoglobin Porto Alegre: ser replaced by cys at position 9 on beta chain
hemoglobin Potomac: glu replaced by asp at position beta101 (g3)
hemoglobin Prato: arg replaced by ser at alpha31(b12): from a calabrian family (southern italy)
hemoglobin Presbyterian: low oxygen affinity; asn replaced by lys at position beta 108(g10)
hemoglobin Puttelange: a variant with an alanine to valine substitution at residue beta 140
hemoglobin Pyrgos: asp replaced by gly at position 83(ef7) on the beta chain
hemoglobin Quebec-Chori: threonine replaced by isoleucine in position beta f3; found in patient with sickle cell disease
hemoglobin Queens: leu replaced by arg at position 34(b12) on alpha chain
hemoglobin Queens Park: lysine replaces methionine at position 32(b13) of the alpha chain
hemoglobin Questembert: ser replaced by pro at alpha131(h14) position
hemoglobin Quin-Hai: leu replaced by arg at position 78(ef2) on beta chain
hemoglobin Quong Sze: ctg replaced by ccg at coden 125 on alpha chain
hemoglobin Radcliffe: ala replaced by asn at position 99 on beta chain
hemoglobin Rahere: lys replaced by thr at position beta82(ef6); the 2,3-diphosphoglycerate binding site
hemoglobin Rainier: tyr replaced by cys at position 145 on beta chain; abnormality induced by ethylnitrosourea
hemoglobin Raleigh: beta1(na1)val replaced by ac-ala; found in swedish diabetic patients
hemoglobin Rambam: aspartic acid replaces glycine at position 69(e13) of beta chain, in addition to beta(0)-thalassemia
hemoglobin Ramona: tyrosine replaced by cysteine at position 24(b5) of alpha1 chain
hemoglobin Rancho Mirage: substituted asp for his at position beta 143(h21); variant in the 2,3-diphosphoglycerate binding site; shows normal oxygen affinity at physiological ph
hemoglobin Randwick: unstable beta chain hemoglobin variant; try replaced by gly on beta chain 15(a12)
hemoglobin Redondo: his replaced by asn at position beta 92(f8)
hemoglobin Regina: leu replaced by val at position beta96(fg3); causes mild erythrocytosis
hemoglobin Reims: glu replaced by gly at position alpha23(b4); alpha chain variant with slightly decreased stability
hemoglobin Riccarton: glycine at position 51 of alpha-chain replaced by serine
hemoglobin Rio Claro: methionine replaces valine at position 34(b16) of the beta subunit
hemoglobin Rio Grande: lys replaced by thr at position 8 (a5) on beta chain
hemoglobin Riverdale-Bronx: gly replaced by arg at position 24(b6) on beta chain
hemoglobin Riyadh: lysine replaced by asparagine at position 120 of beta chain
hemoglobin Roanne: a hemoglobin variant with the asp at alpha 94 (g1) replaced by glu
hemoglobin Roseau-Pointe a Pitre: glu replaced by gly at alpha(2)beta(2)90(f6); displayed instability & low blood oxygen affinity; may be present inassociation with a beta thalassemia trait
hemoglobin Rothschild: try replaced by arg at position 37(c3) on beta chain; for structure & functional studies, see febs lett 1977;82(2):243
hemoglobin Roubaix: leucine replaces valine at position 55 of the e4 chain of the alpha subunit
hemoglobin Rouen: an alpha-chain variant with a substitution of his for tyr at position 140(hc2)
hemoglobin S Providence: hb a-like sickle hemoglobin; glutamic acid replaced by valine on beta6 & lysine replaced by asparagine on position 82
hemoglobin S-Antilles: beta6-glu replaced by val and beta23 val replaced by ile
hemoglobin S-Cameroon: a variant with two amino acid substitutions (beta6(a3)glu to val) and (beta90(f6)glu to lys)
hemoglobin S-Clichy: valine replaces glutamate at position 6(a3) of the beta-chain and threonine replaces lysine at position 8(a5) of the beta-chain
hemoglobin S-Oman: beta6 glu replaced by val and beta121 glu replaced by lys resulting in a dominant sickle syndrome
hemoglobin S-San Martin: valine replaces glutamic acid at position 6(a3) of the beta-chain and proline replaces leucine at position 105(g7) of the beta-chain
hemoglobin S-south end: hb s variant hemoglobin, hb s-south end (beta glu6val, gag to gtg; beta lys132asn, aaa to aac)
hemoglobin SAD: artificially engineered mutant hemoglobin combining the mutant features of hb s antilles and hb d punjab
hemoglobin Saale: ala replaced by thr at position 84(ef8) of the beta chain
hemoglobin Sabine: unstable; leu replaced by pro at position alpha2 beta 2 91(f7)
hemoglobin Sagami: a hemoglobin variant, detected by electrospray ionization mass spectrometry; an abnormal peptide was found in digests of non-dervatized globin 13 da smaller than beta t14
hemoglobin Saint Etienne: glutamine replaces histidine at position 92(f8) of beta chain
hemoglobin Saint Jacques: ala replaced by thr at position alpha2 beta2 140(h18); high oxygen-affinity variant with altered bisphosphoglycerate binding
hemoglobin Saint Mande: asn replaced by tyr at position 102 on beta chain
hemoglobin Saint Nazaire: phe replaced by ile at position beta103(g5)
hemoglobin Sainte Eugenie: beta104(g6)arg replaced by trp
hemoglobin Sainte Seve: results from the frameshift mutation at codon 118 (-t)
hemoglobin Saitama: histidine replaced by proline at position 117 (g19) on beta chain
hemoglobin Sallanches: tyrosine replaces cysteine at position 104(g11) of the alpha subunit
hemoglobin Santa Clara: asparagine replaces histidine at position 97(fg4) of the beta chain
hemoglobin Santander: aspartic acid replaces valine at position 34(b16) of beta chain
hemoglobin Saratoga Springs: asparagine replaces lysine at position 40(c5) of the alpha chain
hemoglobin Sarrebourg: found in a spanish family with mutation beta131(h9)gln replaced by arg (cag replaced by cgg)
hemoglobin Saskatoon: glu replaced by ala at position 22 on beta chain; hb m saskatoon have the alpha2 his at position 63 replaced by beta2 tyr
hemoglobin Sassari: causes distinc erythrocytosis; asp replaced by his(beta2) at alpha(2)126(h9) position
hemoglobin Savaria: ser replaced by arg at position alpha2(49)beta2(ce7)
hemoglobin Saverne: beta chain composed of 156 amino acid residues; unstable, high affinity variant with low cooperativity
hemoglobin Schlierbach: isoleucine replaces asparagine at position 108(g10) of the beta subunit
hemoglobin Seal Rock: terminal codon is replaced by glutamate at position 142 of the alpha2 chain
hemoglobin Sealy: asp replaced by his at position 47 on the alpha chain
hemoglobin Seattle: beta70(e14)-ala replaced by asp; do not confuse with hemogloblin f seattle
hemoglobin Sendagi: phe replaced by val at position 42 on beta chain
hemoglobin Senegal: the senegal 5'beta-haplotype and the polymorphism at -158 of g(gamma) was linked to the high-hbf (fetal hemoglobin) phenotype
hemoglobin Shaare Zedek: lys replaced by glu at position 56 on alpha chain