Genetic control of gamma chain synthesis: A chemical and evolutionary study of the Gm(a) factor of immunoglobulins

Wang, An-Chuan; Fudenberg, H. Hugh

doi:10.1016/0022-2836(69)90375-1

Cited by 32 publications

(8 citation statements)

References 14 publications

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“…Similar studies [Alepa, 1968;Shuster et al, 1969;Vyas and F udenberg, 1969;Wang and F udenberg, 1969] indicated a lack of human IgG subclass determinants in the lower primate species, including gibbons (Hylobatidae), Old World monkeys (Cercopithecidae), New World monkeys (Ceboidea), and prosimians (Prosimii). Further confirmation was obtained by the immunization of various lower primates with human IgG, the resulting antisera having specificity for human-type IgG subclass deter minants [Dray, 1960;Lichter and Dray, 1964;Terry and Fahey, 1964;G rey andKunkel, 1964, 1967;Yount et al, 1967;Vyas and Fudenberg, 1969] .…”

Section: Introductionmentioning

confidence: 72%

“…As mentioned above, abundant evidence supports the notion that the great apes possess the hu man-type IgG subclass determinants. Wang and F udenberg [1969] tested for the presence of human IgG3-type immunoglobulins in the plasma of 6 species of New World monkeys, with negative results. It would, therefore, appear that ceboid monkeys, as do other lower primates, lack the humantype IgG subclass determinants and, in addition, from the present results, lack the Old World monkey-type IgG subclass determinants as well.…”

Section: Discussionmentioning

confidence: 99%

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The Occurrence of Baboon-Type IgG Subclass Antigenic Determinants within the Order Primates

Damian¹,

Luker²,

Greene³

et al. 1972

IJFP

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Sera from a large variety of nonhuman primates were tested for baboon-type IgG subclass determinants by immunoelectrophoresis. Specific rabbit antisera to savanna baboon γ-chains, unreactive with human IgG, and capable of differentiating 4 baboon IgG subclasses were used in this study. Frosimian and ceboid IgG’s were unreactive, as were the IgG’s of the great apes (chimpanzee, gorilla, and orang-utan). Cercopithecid monkeys fell into species groups, according to the extent of their IgG correspondence to baboon IgG, with langur monkey IgG being the most dissimilar. A sharing of subclass determinants between gibbon IgG and baboon IgG was revealed. Evidence for multiple IgG(B2) determinants was also found. The phylogenetic distribution of baboon-type and human-type IgG subclass determinants within the primate order is traced.

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Section: Introductionmentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

The Occurrence of Baboon-Type IgG Subclass Antigenic Determinants within the Order Primates

Damian¹,

Luker²,

Greene³

et al. 1972

IJFP

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“…For two-dimensional peptide mapping on filter paper, each digest was subjected to high vol tage electrophoresis followed by descending chro matography at a 90 angle in a chromatography tank. The detailed conditions for peptide mapping were as described previously [31], The peptide maps were dried and stained with 0.2°/o ninhydrin in acetone.…”

Section: Methodsmentioning

confidence: 99%

Coexistence of Multiple Monoclonal Immunoglobulins with Identical Constant Regions in One Patient

1982

Self Cite

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Two populations of IgG molecules, designated F-IgG3(χ) and S-IgG3(χ), were isolated from a patient with multiple myeloma. The constant regions of the two molecules appear to be identical, since the heavy chains of both belong to the γ³ subclass and both molecules are positive for G3m(5), G3m(10), and G3m(ll) but negative for G3m(21), Km(l) and Km(2) allotypes. In contrast, the two molecules have different variable regions, since (a) they do not share idiotypic determinant(s); (b) their light chains have different NH₂ terminal amino acid sequences, and (c) both their heavy and light chains have different peptide maps and amino acid compositions. SDS-polyacrylamide gel electrophoresis showed that the F-IgG3(χ) molecules have two kinds of light chains. One, designated χn, has a normal molecular weight (approximately 23,000); the other, designated χh, has a molecular weight of approximately 28,000.

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“…The purified cold agglutinins were reduced by 0.01 m dithiothreitol and alkylated by a 50-percent molar excess of iodoacetamide as described earlier [25]. Separation of heavy and light chains was performed on a Sephadex G-100 column using 1 m acetic acid as eluent.…”

Section: Methodsmentioning

confidence: 99%

Chemical Analyses of Variable Regions of Heavy and Light Chains of Cold Agglutinins1

Gergely¹,

Wang²,

Fudenberg³

1973

Vox Sanguinis

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The variable regions of cold agglutinins with anti-I and anti-Pr specificities were investigated by N-terminal amino acid sequencing and by analyses of pyrrolidonecarboxylic acid-blocked peptides after digestion of polypeptide chains with Nargase. Results showed that the heavy chains of four IgM anti-I cold agglutinins are exclusively VHI subgroups and their light chains are exclusively VKII subgroup. In contrast, the light chains of two cold agglutinins with anti-Pr specificity are not VKII, while their heavy chains are not restricted to a single subgroup. The amino acid sequences at the first hypervariable region of light chains (positions 25- 35) are similar in two of the four anti-I cold agglutinins. These sequences are different from that of the light chain of another cold agglutinin with anti-Pr specificity. These results support the concept that only antibodies with the same specificity can share similar primary structure at their antigen combining sites.

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Genetic control of gamma chain synthesis: A chemical and evolutionary study of the Gm(a) factor of immunoglobulins

Cited by 32 publications

References 14 publications

The Occurrence of Baboon-Type IgG Subclass Antigenic Determinants within the Order Primates

The Occurrence of Baboon-Type IgG Subclass Antigenic Determinants within the Order Primates

Coexistence of Multiple Monoclonal Immunoglobulins with Identical Constant Regions in One Patient

Chemical Analyses of Variable Regions of Heavy and Light Chains of Cold Agglutinins1

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