bluuebunny/crossref_metadata_2025_split huggingface dataset:
THE ROLE OF DISULFIDE BONDS IN THE COMPLEMENT-FIXING AND PRECIPITATING PROPERTIES OF 7S RABBIT AND SHEEP ANTIBODIES
Authors: Schur Peter H. , Christian Gary D. 
Published: June 2004

The number of total disulfide bonds in rabbit and sheep 7S gamma globulin, before and after treatment with 2-mercaptoethanol, has been measured by amperometric titration.
Mercaptan reduction could diminish the complement-fixing efficiency of 7S rabbit gamma globulin by no more than 90 per cent without any significant decrease in maximal complement-fixing ability. This was associated with the reduction of only 7 disulfide bonds, including 1 interchain disulfide bond [S—S(1)].
The reduction of 7 disulfide bonds in 7S sheep gamma globulin was associated with a 64 per cent decrease in complement-fixing efficiency, while reduction of 10 to 11 disulfide bonds decreased the complement-fixing efficiency by 90 per cent. Reduction of more disulfide bonds was not associated with any further decrease in complement-fixing efficiency, nor of any decrease in maximal complement-fixing ability.
The reduction of more than 10 to 11 disulfide bonds in 7S rabbit and sheep gamma globulins was associated with a decrease in precipitating ability.
The disulfide bonds which are more labile to mercaptan reduction appear to be associated with complement-fixing efficiency while the disulfide bonds which are more resistant to mercaptan reduction appear to be associated with precipitating ability.
The measurement of interpolypeptide chain disulfide bonds has been discussed. One easily reduced interchain disulfide bond [S—S(1)] appears to be important for the complement-fixing efficiency of 7S rabbit antibody. The integrity of this same bond is essential for the precipitating ability of 5S rabbit antibody and may also be important for its complement-fixing ability.
IMMUNOLOGICAL AND BIOCHEMICAL STUDIES ON SERUM HAPTOGLOBIN
Authors: Shim Bong-Sop , Bearn Alexander G. 
Published: June 2004

Antibody to purified type 1-1 human serum haptoglobin was obtained in rabbits. Using this antiserum it was demonstrated that the antigenic determinants of the haptoglobin molecule reside in both α- and ß-chains. No immunological difference between the normal α1F- and α1S-chains of haptoglobin could be detected.
A number of healthy individuals whose haptoglobin pattern appeared normal by starch gel electrophoresis were shown to possess a haptoglobin which could be distinguished immunologically from the common haptoglobin types. These immunological atypical haptoglobins have been observed in individuals of types 1-1, 2-1, and 2-2. Combined immunological and chemical studies of purified haptoglobin have enabled the construction of a tentative model for the structure of human type 1-1 haptoglobin.
SEROLOGIC STRAIN DIFFERENTIATION IN TRACHOMA
Authors: Nichols Roger L. , McComb Dorothy E. 
Published: June 2004

An in vitro test for the differentiation of trachoma strain isolates was described. The method was based on absorption of trachoma antiserum followed by immunofluorescent staining of individual trachoma strains.
Nineteen trachoma strains were studied; two main types were identified. Evidence for quantitative and qualitative antigenic variation between the two types was presented. The limitations in practice and in theory of the test were emphasized.
A STUDY OF RABBIT γ-GLOBULIN ALLOTYPY BY MEANS OF HETEROIMMUNIZATIONS
Authors: Bornstein Paul , Oudin Jacques 
Published: June 2004

Representatives of two species, the chicken and the goat, were immunized by injection with Freund's adjuvant, of specific precipitates prepared from the antisera of rabbits with various allotypic specificities. The precipitation reactions of the resulting antisera with normal rabbit sera were studied in liquid and in gellified media. In these reactions the isotypic specificity and often one or the other of the allotypic specificities of rabbit γ-globulin were involved.
It was always easier to obtain antibodies against the specificities controlled by the alleles of locus b (Ab4, Ab5, Ab6) than of locus a (Aa1, Aa2, Aa3). The precipitation reaction of antibodies against a specificity of the a series could always be inhibited by an excess (nearly always moderate) of a serum lacking this specificity. A similar inhibition of the antibodies against the specificities of the b series was often impossible, especially if the antiserum had been collected after a second injection of immunizing material.
The reactions of 58 Ab4+ sera with a goat anti-Ab4 serum and of 28 Ab5+ sera with a chicken anti-AbS serum were studied in gel tubes (simple diffusion). The constant observation of two precipitation zones due respectively to two types of molecules, Ab4+ and Ab4- (or Ab5+ and Ab5-), indicated the existence of an appreciable number of Ab4- or Ab5- molecules, even in supposed homozygotes. In the latter rabbits Ab4- or Ab5- molecules are b- molecules; i.e., molecules lacking the specificities of the b series. Measurements of the distances between the two zones in the reaction of 72 sera revealed significant differences between sera of individuals of the same phenotype, as well as systematic differences not only between sera of homozygotes and of heterozygotes, but also between heterozygotes of different genotypes. These measurements were used to evaluate the ratio of concentrations of the two types of molecules detected by each of the two antisera.
The occurrence of b- molecules in every one of the fairly large number of sera studied indicates a new aspect of the heterogeneity of γ-globulin. Although detected by means of allotypy, this heterogeneity is not dependent upon factors which vary with individuals.
These results are discussed in connection with what is known of the structure of γ-globulin.
NATURALLY OCCURRING HUMAN ANTIBODY REACTING WITH BENCE JONES PROTEINS
Authors: Epstein Wallace V. , Gross Dale 
Published: June 2004

Agglutinating substances having characteristics of naturally occurring macroglobulin antibodies to human Bence Jones proteins have been identified in human sera. By means of hemagglutination and hemagglutination inhibition techniques, common determinants have been demonstrated on the light (L) polypeptide chains of pooled normal human γ2-globulin and on some Bence Jones proteins of group 1 but not of group 2. Individual human sera serve to delineate subgroups of the two major antigenic groups of the Bence Jones proteins by agglutinating cells coated by one but not another protein of the same antigenic group. The complexity of subgroups, especially of group 2, is established by testing a panel of Bence Jones proteins of the same group for their ability to inhibit hemagglutination. By this means it appeared that different sera recognized different group-specific determinants of cells coated with a single Bence Jones protein.
The capacity of the L polypeptide chains and proteolytic fragments of γ2-globulin to inhibit the hemagglutination reaction between Bence Jones protein or L chain-coated cells and human sera was examined. These studies demonstrated that the determinants, toward which agglutinators of human serum are directed, appear to be blocked in intact γ2-globulin and in all fragments in which H chain remains in proximity to L chain. It would appear that the presence of H chains bound to L chains by non-covalent bonds completely obstructs the reactivity of the involved L chain groups. The agglutinating capacity of a serum toward Bence Jones proteins or L chains of γ2-globulin appeared to be independent of its agglutinating capacity for cells coated with intact γ2-globulin. No correlation of the presence in serum of agglutinators for Bence Jones proteins or L chains with health or disease has been established.
RECOMBINATION OF ANTIBODY POLYPEPTIDE CHAINS IN THE PRESENCE OF ANTIGEN
Authors: Metzger Henry , Mannik Mart 
Published: June 2004

Conditions were developed by which the separated H and L chains of gamma2 globulins recombined to form four-chained molecules in good yields.
In the absence of antigen, anti-2,4-dinitrophenyl (anti-DNP) H chains randomly reassociated with a mixture of antibody and non-specific gamma2 globulin L chains. In the presence of a specific hapten, however, the antibody H chains preferentially interacted with the anti-DNP L chains.
Antibody H chain-antibody L chain recombinants formed in the presence of hapten were more active than the corresponding recombinants formed in the absence of hapten.
Speculations are made regarding the possible mechanisms and biological significance of these effects.
RESISTANCE OF THE MOUSE'S INTESTINAL TRACT TO EXPERIMENTAL SALMONELLA INFECTION
Authors: Bohnhoff Marjorie , Miller C. Phillip , Martin William R. 
Published: June 2004

Determinations of pH, Eh, and concentrations of acetic, butyric and lactic acids were made on the content of cecum and transverse colon of groups of mice killed 1, 3, and 5 days after oral administration of 50 mg streptomycin. Control observations on untreated mice are reported in the preceding communication. Heat-killed supenatants of suspensions of bowel content were tested in vitro for their ability to inhibit multiplication of our standard streptomycin-resistant strain of Salmonella enteritidis during aerobic and anaerobic incubation. Also tested in like fashion were series of cultures in broth buffered at various pH levels and containing acetic, butyric, and lactic acids in varying concentrations.
In colon content of mice on the 1st day after streptomycin treatment, the pH had risen and the concentrations of the fatty acids fallen, a combination of effects which adequately accounts for its inability to inhibit multiplication of Salmonella in vitro and in vivo. By the 3rd day after streptomycin treatment, pH and fatty acid concentrations had returned to normal levels. The susceptibility of mice to oral challenge on the 3rd day was explained by the finding that lactic acid had accumulated in colon content to levels which, in broth, effectively counteracted the activity of inhibitory concentrations of the fatty acids. Other cocarboxylic acids also antagonized the inhibitory activity of the fatty acids; glucose did not.
INTERFERENCE WITH IMMUNE HEMOLYSIS BY GLYCOPROTEIN ANTIGENS
Authors: Arquilla E. R. , Hamlin J. , Hamashige S. , Miller A. 
Published: June 2004

1. The titer of an individual insulin antiserum measured by hemagglutination agrees favorably with the titer of the same antiserum as measured by immune hemolysis.
2. In contrast, a marked decrease is noted in the immune hemolysis titers relative to hemagglutination titers of antisera prepared against three different sialic acid-containing proteins (human chorionic gonadotropin, rabbit transferrin, and human transferrin).
3. The lower immune hemolytic titers of glycoprotein antisera are apparently not due to a lack of complement-fixing γ2-antibodies.
4. The glycoprotein antigens in solution do not interfere with hemolysis in the insulin immune system.
5. By contrast, marked inhibition of insulin immune hemolysis occurs when cells are sensitized with both glycoprotein and insulin.
6. Cells treated with neuraminidase (to remove cell surface sialic acid) lyse in the presence of C'a alone.
7. If neuraminidase-treated cells are sensitized with sialic acid-containing protein, the lysis of these cells by complement is inhibited.
8. It is, therefore, postulated that during some initial phase of immune hemolysis, a sialic acid-containing substrate is cleaved from the cell surface, rendering the cell susceptible to lysis. If this removal is interfered with, i.e., by sensitization of the cell with competitive sialic acid-containing antigen, then the lytic portion of immune hemolysis cannot proceed.
STUDIES OF TUBERCLE BACILLUS-HISTIOCYTE RELATIONSHIPS
Authors: Fong Jacob , Chin Dennis , Elberg Sanford S. 
Published: June 2004

Comparison of the Brucella-immune and the BCG-immune histiocyte, each of which is resistant to necrotization by either Brucella or mycobacteria, has revealed a number of dissimilarities in their behavior. The Brucella-immune histiocyte was found to be incapable of transferring its resistance to the cells of normal animals; it was also unable to achieve attenuation of virulent tubercle bacilli. In contrast, the BCG-immune histiocyte and certain of its subcellular components (ribosomes and ribosomal RNA) were effective in inducing cellular resistance in normal animals against both Brucella and mycobacteria. When RNA was used, only immune ribosomal RNA was effective; when intact ribosomes were used, both immune and recipient ribosomes proved active.
These investigations have also shown that the resistance of the BCG-immune histiocyte against Brucella and mycobacteria was of long duration and not readily dissociable.
DISTRIBUTION, INHERITANCE, AND PROPERTIES OF AN ANTIGEN, MUB1, AND ITS RELATION TO HEMOLYTIC COMPLEMENT
Authors: Cinader B. , Dubiski S. , Wardlaw A. C. 
Published: June 2004

An antigen, MuB1, present in the sera of some mice, can elicit a precipitating antibody in certain other strains of mice. An antibody to the antigen MuB1 can also be elicited in rabbits. 99 strains and substrains of inbred mice were tested for the presence of MuB1; the antigen was found in the sera of 44 strains (61 per cent) and 14 DBA substrains (52 per cent). Evidence is presented indicating that mice lacking MuB1 do not make a modified antigen, corresponding to MuB1, but are genetically deficient in synthetic ability at this site.
By reaction with antibody to MuB1 an antigen corresponding to MuB1 was found in 13 of the 15 orders of mammals, and in 63 of 85 mammalian species tested, including man and guinea pig.
The quantity of the antigen MuB1 is always greater in the serum of male than in the serum of female mice. The concentration of MuB1 increases with age; this increase is more marked in male than in female mice.
By means of backcross experiments it was shown that the inheritance of MuB1 is unifactorial, is independent of the inheritance of the gamma globulin allotype MuA2, and is qualitatively independent of the sex of the parents.
The antigen MuB1 is found in the euglobulin fraction of serum; it loses its ability to precipitate with antibody after heating at 56°C, but not after treatment with ammonia or hydrazine. By gel filtration, MuB1 is separated with a fraction containing molecules of molecular weight ≈ 150,000.
An empirical correlation was observed between the presence or absence of MuB1 in the sera from inbred mice and the presence or absence of hemolytic complement (Hc), as measured by a test using a high concentration of rabbit hemolysin. In backcross experiments also, a correlation between hemolytic complement and the presence of MuB1 was demonstrated. As with MuB1, male mice had a higher hemolytic complement level than females. The particular component of complement which may be identical with MuB1 has not been identified.
EVIDENCE FOR SPECIES' DIFFERENCES IN THE EFFECT OF SERUM γ-GLOBULIN CONCENTRATION ON γ-GLOBULIN CATABOLISM
Authors: Sell Stewart 
Published: June 2004

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig γ-globulins and human serum albumin were determined in mice and in guinea pigs whose serum γ-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum γ-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled γ-globulins from all species tested were markedly increased in mice with elevated γ-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit γ-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine γ-globulin were only partially effective, and injections of human serum albumin had no effect. The γ-globulin catabolic rates were decreased in mice with subnormal serum γ-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum γ-globulin levels. In contrast, elevation of the serum γ-globulin levels by injections of exogenous γ-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled γ-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum γ-globulin concentration appears to be operative in the mouse, but not in the guinea pig.
Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum γ-globulin levels.
ENDOSYMBIOTIC RELATIONSHIP BETWEEN ANIMAL VIRUSES AND HOST CELLS
Authors: Fernandes Mario V. , Wiktor Tadeusz J. , Koprowski Hilary 
Published: June 2004

RE cultures infected with a fixed rabies virus were studied. The virus can propagate itself in these cells for an indefinite period of time without interfering with cell growth. The present study characterizes this truly endosymbiotic relationship.
Virus-specific antigen was detected in the cytoplasm of each cell by fluorescein-labeled antirabies serum but only 4 to 5 per cent of the cells released infectious virus. All cells undergoing division showed viral antigen throughout the mitotic process. Also, the growth rate, plating efficiency, and morphological characteristics of both the infected and control cultures were identical. No difference was detected between the RE and the RE-CVS cell populations by RNA and DNA labeling experiments, using H3-thymidine, and H3-uridine. Although antirabies serum effectively inhibited the spread of extracellular virus, it did not interfere with cell-to-cell transmission of the virus during mitosis, in the course of 9 cell transfers during 53 days. RE-CVS cells, when exposed to fresh antirabies serum, lysed completely but inactivated serum had no lytic effect. The addition of fresh hamster complement to the inactivated serum restored its cytolytic properties.
The serially passaged RE-CVS virus gradually became less virulent for mice and displayed a weak antigenicity in the mouse protection test.
Another feature of the RE-CVS cell system is its resistance to infection with homologous and heterologous viruses despite the apparent absence of an interferon-like substance.
TRANSPORT OF GLOBIN BY THE RENAL GLOMERULUS
Authors: Menefee Max G. , Mueller C. Barber , Bell Allen L. , Myers Joseph K. 
Published: June 2004

Purified human globin injected into rats forms aggregates which are identifiable by their characteristic appearance in thin sections in the electron microscope and by their positive autoradiographs when the globin is tritiated before injection. Globin is taken up by endothelial cells of glomerular capillaries and is transported across the cell within the limits of a surrounding membrane. Globin is rarely seen to pass through fenestrations. Globin is also taken into the stalk region where it is seen usually within the sponge fibers and only occasionally within stalk cells. Globin is seen in all stages of passage through the basement membranes and sponge fibers, which are not deformed by its passage. On the basis of the findings presented here and by others, it is postulated that the basement membrane and sponge fibers consist of a thixotrophic gel.
After traversing the basement membrane, the globin passes between foot processes of the epithelial cells. The slit membranes are deformed by this passage and thus appear to be distinctive structures. The globin is next found free in Bowman's space; the earliest aggregates are seen there within 1 minute after injection.
Globin taken up in the stalk region is slowly discharged and very little is found there 6 hours postinjection.
EXPERIMENTAL STUDIES IN ACUTE RENAL FAILURE
Authors: Menefee Max G. , Mueller C. Barber , Miller Tracy B. , Myers Joseph K. , Bell Allen L. 
Published: June 2004

When purified human globin is injected intravenously into rats it produces acute renal failure characterized by tubular casts and oliguria. The globin is identifiable within vesicles and channels in the cytoplasm of the proximal tubules, through which it passes from lumen to basal side with no apparent serious effect on the cells. When a very minimal amount of globin is taken up by cells of the distal limb of Henle's loop or distal tubules (lower nephron), a markedly deleterious effect is apparent and the cells die within a short time. The mixture of cell debris and precipitated globin forms plugs within the confines of the basement membranes of the former distal limbs and distal tubules. After a number of lower nephrons are plugged a disruption of proximal tubules is found, which apparently results from the effect of back pressure in the obstructed nephrons.
We suggest that any amount in excess of a low threshold of globin, either alone or combined with heme or related material, has a toxic effect on lower nephron cells. Once initiated, the toxic effect is not reversible and the resulting plug of debris and precipitate will occlude the lumen. If a sufficient number of nephrons are made non-functional the animal becomes anuric; otherwise it is oliguric. A high rate of urine flow will protect against the excess absorption of material and thus against acute renal failure.
ACTIVITY OF DISSOCIATED AND REASSOCIATED 19S ANTI-γ-GLOBULINS
Authors: Schrohenloher Ralph E. , Kunkel Henry G. , Tomasi Thomas B. 
Published: June 2004

19S anti-γ-globulins were isolated in a high state of purity from the sera of two patients with rheumatoid arthritis. Following reduction with ethyl mercaptan and alkylation by iodoacetamide, fragments were produced which retained the capacity to combine with 7S γ-globulin.
The fragments from one of the 19S anti-γ-globulins agglutinated red cells coated with incomplete anti-Rh antibodies. This activity was shown by density gradient ultracentrifugation to be associated with low molecular weight fractions. The agglutination of the coated red cells by the fragments was strongly inhibited by normal and myeloma 7S γ-globulins and showed a greater specificity than the parent 19S material.
Analytical ultracentrifuge experiments demonstrated that the fragments from either of the 19S anti-γ-globulins formed complexes with 7S γ-globulin.
Reassociation of the dissociated fragments through reformation of disulfide bonds resulted in the formation of fast sedimenting molecules having properties similar to those of the untreated 19S material in respect to precipitation with aggregated γ-globulin and agglutination of coated red cells.