title: The Truth About Stories: A Native Narrative By Thomas King

authors: Douglas, Zanna

abstract: The truth about stories is that that’s all we are.” Koinei ngā kupu e tika ana hei whakamana i te āhua o te pukapuka nei nā Thomas King i tuhi. Ko te pakiwaitara tētehi āhuatanga e pupuri nei e te iwi taketake, he huarahi e mārama ai tātou ki te huringa o te ao. He taonga hoki ēnei kua take mai nō mua rā anō, kia kore e warewaretia wā tātou hītori, kia pupuri tonu hoki ki ngā kōrero ō mua, ngā kōrero e puawai ai te tuakiri o te tangata. Mō King, ka hanga te pakiwaitara i te tangata, nā koianei te pūtakenga mai o tāna aronga i roto i te pukapuka nei. Ko tāna he whakatakoto mai i ngā pakiwaitara kua rangona e ia i roto i ōna tau, me kī ko ngā hītori nō tōna iwi. Ko tētehi o ngā āhuatanga matua ka tū mai i roto i te tuhituhinga nei ko tāna kōrero mō ngā āhuatanga kua pā ki a ia i roto i tōna oranga. He huarahi pai tēnei hei whakamahana atu i te kaituhi ki te kaipānui, mā reira e āhei ana te kaipānui ki te whakawhanaunga atu ki te ngako o ngā kōrero o roto i te pukapuka.

text: The Truth About Stories: A Native Narrative By Thomas King The truth about stories is that that’s all we are.” Koinei ngā kupu e tika ana hei whakamana i te āhua o te pukapuka nei nā Thomas King i tuhi. Ko te pakiwaitara tētehi āhuatanga e pupuri nei e te iwi taketake, he huarahi e mārama ai tātou ki te huringa o te ao. He taonga hoki ēnei kua take mai nō mua rā anō, kia kore e warewaretia wā tātou hītori, kia pupuri tonu hoki ki ngā kōrero ō mua, ngā kōrero e puawai ai te tuakiri o te tangata. Mō King, ka hanga te pakiwaitara i te tangata, nā koianei te pūtakenga mai o tāna aronga i roto i te pukapuka nei. Ko tāna he whakatakoto mai i ngā pakiwaitara kua rangona e ia i roto i ōna tau, me kī ko ngā hītori nō tōna iwi. Ko tētehi o ngā āhuatanga matua ka tū mai i roto i te tuhituhinga nei ko tāna kōrero mō ngā āhuatanga kua pā ki a ia i roto i tōna oranga. He huarahi pai tēnei hei whakamahana atu i te kaituhi ki te kaipānui, mā reira e āhei ana te kaipānui ki te whakawhanaunga atu ki te ngako o ngā kōrero o roto i te pukapuka.

year: 2011-04

title: Ka Pū Te Ruha, Ka Hao Te Rangatahi: Maori identities in the twenty-first century

authors: Kukutai, Tahu

abstract: These social divides and problems are at the heart of this text.

text: Ka Pū Te Ruha, Ka Hao Te Rangatahi: Maori identities in the twenty-first century These social divides and problems are at the heart of this text.

year: 2017-02

title: Characterization of a chelator-resistant proteinase from Thermus strain Rt4A2

authors: Freeman, S.A.

subjects: thermos

abstract: The Thermus isolate Rt4A2 was found to produce an extracellular chelator-resistant proteinase. The proteinase was purified to homogeneity by (NH4)2SO4 precipitation, cation-exchange chromatography, gel-filtration chromatography, and weak anion-exchange chromatography. The Rt4A2 proteinase was found to have properties typical of an alkaline serine proteinase. It had a pH optimum of 9.0 and was specifically inhibited by phenylmethanesulphonyl fluoride. Its isoelectric point was greater than 10.25. Its molecular-mass was 31.6 kDa as determined by SDS/PAGE. N-terminal sequencing has shown it to have high sequence similarity with other serine proteinases from Thermus species. The proteinase hydrolysed a number of substrates including fibrin, casein, haemoglobin, collagen, albumin and the synthetic chromogenic peptide substrate Suc-Ala-Ala-Pro-Phe-NH-Np. The specific activity of the purified proteinase using azocasein as substrate was 313 units/mg. Substrate inhibition was observed above an azocasein concentration of 0.05% (w/v). Esterase activity was directed mainly towards those substrates containing the aliphatic or aromatic residues of alanine, glycine, tryptophan, tyrosine and phenylalanine. Thermostability half-lives of greater than 7 days at 70 degrees C, 43 h at 80 degrees C and 90 min at 90 degrees C were found in the presence of 5 mM CaCl2. At 90 degrees C increasing the CaCl2 concentration 100-fold (0.5 mM to 50 mM) caused a 4.3-fold increase in the half-life of the enzyme from 30 to 130 min. Half-lives of 19.4 min at 100 degrees C and 4.4 min at 105 degrees C were found in the presence of 50 mM CaCl2. The metal chelators EGTA and EDTA reduced the stability at higher temperatures but had no effect on the activity of the proteinase. Activity was not stimulated by common metal activators such as Ca2+, Mg2+ and Zn2+.

text: Characterization of a chelator-resistant proteinase from Thermus strain Rt4A2 The Thermus isolate Rt4A2 was found to produce an extracellular chelator-resistant proteinase. The proteinase was purified to homogeneity by (NH4)2SO4 precipitation, cation-exchange chromatography, gel-filtration chromatography, and weak anion-exchange chromatography. The Rt4A2 proteinase was found to have properties typical of an alkaline serine proteinase. It had a pH optimum of 9.0 and was specifically inhibited by phenylmethanesulphonyl fluoride. Its isoelectric point was greater than 10.25. Its molecular-mass was 31.6 kDa as determined by SDS/PAGE. N-terminal sequencing has shown it to have high sequence similarity with other serine proteinases from Thermus species. The proteinase hydrolysed a number of substrates including fibrin, casein, haemoglobin, collagen, albumin and the synthetic chromogenic peptide substrate Suc-Ala-Ala-Pro-Phe-NH-Np. The specific activity of the purified proteinase using azocasein as substrate was 313 units/mg. Substrate inhibition was observed above an azocasein concentration of 0.05% (w/v). Esterase activity was directed mainly towards those substrates containing the aliphatic or aromatic residues of alanine, glycine, tryptophan, tyrosine and phenylalanine. Thermostability half-lives of greater than 7 days at 70 degrees C, 43 h at 80 degrees C and 90 min at 90 degrees C were found in the presence of 5 mM CaCl2. At 90 degrees C increasing the CaCl2 concentration 100-fold (0.5 mM to 50 mM) caused a 4.3-fold increase in the half-life of the enzyme from 30 to 130 min. Half-lives of 19.4 min at 100 degrees C and 4.4 min at 105 degrees C were found in the presence of 50 mM CaCl2. The metal chelators EGTA and EDTA reduced the stability at higher temperatures but had no effect on the activity of the proteinase. Activity was not stimulated by common metal activators such as Ca2+, Mg2+ and Zn2+.

year: 1993