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Sequence studies on the constant region of the Fd sections of rabbit immunoglobulin G of different allotype.

ABSTRACT: The amino acid sequence has been completed for the constant region of the Fd fragments of heavy chains from rabbit IgG (immunoglobulin G) of allotype Aa1 and Aa3. The amino acid sequence given by Fruchter et al. [(1970) Biochem. J. 116, 249-259] for the constant region of the Fd fragment from Aa1 IgG was extended and in in part corrected to give a continuous sequence of 140 residues. No allotype-related sequence variation was found in the constant section of the Fd fragment. This evidence confirms the view that the differences in sequence between the variable regions of Aa1 and Aa3 IgG [Mole et al., (1971) Biochem. J. 124, 301-318] are responsible for the allotypic specificities.

SUBMITTER: Pratt DM

PROVIDER: S-EPMC1172364 | biostudies-other | 1975 Nov

REPOSITORIES: biostudies-other

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Sequence studies of the Fd section of the heavy chain of rabbit immunoglobulin G.

Project description:A partial amino acid sequence was given by Cebra, Steiner & Porter (1968b) of the N-terminal half of the heavy chain of rabbit immunoglobulin G. This was extended and in part corrected to give a continuous sequence of 136 residues, which together with other work accounts for three-quarters of the total sequence. Evidence is given suggesting that there is a limited region of 10-15 residues that are exceptionally variable in the heavy chains from pooled rabbit immunoglobulin G.

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| S-EPMC1198747 | biostudies-other

The primary structure of the constant region of Basilea-rabbit immunoglobulin lambda-chains.

Project description:The amino acid sequence of the constant region of the immunoglobulin lambda-chain of the rabbit (C lambda) has been determined. This chain was obtained from a homogeneous anti-(type II pneumococcal polysaccharide) antibody fraction raised in Basilea rabbit 4548. The C lambda-region sequence was established by the analysis of tryptic and some overlapping chymotryptic peptides and partly by homology with known C lambda-region sequences of lambda-chains from other species. Peptides were isolated by a combination of methods including high-voltage paper electrophoresis, gel filtration and high-pressure liquid chromatography. The peptides were subjected to automated Edman degradation in the presence of Polybrene. The sequence showed no evidence of heterogeneity. Large interspecies similarities, as well as amino acid interchanges, are apparent among various C lambda regions; the degrees of homology between rabbit C lambda region and the C lambda region from human, porcine and murine chains are 72.6, 71 and 72% respectively. The similarity of lambda-chains of different species is much greater than that found between rabbit kappa- and lambda-chains (about 34% homology). Genetic implications of these results are discussed.

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Sequence studies on the heavy chain of rabbit immunoglobulin A of different alpha-locus allotypes.

Project description:The amino acid sequence was determined of part of the variable region of heavy chain from rabbit immunoglobulin A of allotypes a1 and a3. Two corrections of the primary sequence of Aa1 gamma-chains are reported; most of the structural correlates of the alpha-locus allotypes are confirmed. The amino acid sequence of the N-terminal 20 residues of alpha-negative molecules was also determined and found to be homologous to the human VhIII subgroup. These molecules are present in a much higher proportion in the alpha-chain pool than in the gamma-chain.

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Variation in the N-terminal sequence of heavy chains of immunoglobulin G from rabbits of different allotype.

Project description:The sequences of the N-terminal peptides prepared by Pronase digestion of the heavy chain of rabbit immunoglobulin G of allotype Aa1, Aa2 and Aa3 were determined and were shown to be related to the allotype. An N-terminal fragment of about 34 residues was also prepared from the allotype heavy chains, by cleavage with cyanogen bromide; the yield varied with the allotype. The sequences of the cyanogen bromide fragments from the Aa1 and Aa3 heavy chains contain allotype-related variations similar to those found in the N-terminal Pronase peptides, and these sequences are thought to be representative of the whole heavy-chain populations. There is about 60% homology between the two sequences, and superimposed on the differences between them there are a number of positions within each sequence at which at least two amino acids are present.

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Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains.

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Human immunoglobulin subclasses. Partial amino acid sequence of the constant region of a gamma 4 chain.

Project description:The heavy chain of a human myeloma protein (Vin) belonging to the gamma4 subclass was subjected to tryptic digestion after reduction and carboxymethylation. Cyanogen bromide fragments were also prepared and all 19 tryptic peptides that account for one of them (the Fc-like fragment) were studied. Selected peptic peptides were isolated and provided evidence for the order of 15 of the tryptic peptides. In addition the sequence of two large peptic peptides derived from two sections of the molecule including all the interchain bridges is presented. Comparison with published data on other chains allows us to propose a sequence of gamma4 chains that extends from just before the presumed starting point of the invariable region (at about residue 113) to the C-terminal end of the chain (approx. residue 446), except for a section of about 50 residues. The results of the comparison suggest that the immunoglobulin subclasses have a recent independent evolutionary origin in different species. Implications for complement fixation and for the evolutionary origin of antibody diversity are also discussed.

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cDNA clones encoding rabbit immunoglobulin lambda chains. Evidence for length variation of the third hypervariable region and for a novel constant region.

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A novel monoclonal antibody against the constant region of goose immunoglobulin light chain.

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