scholarly journals Cyanogen bromide cleavage and partial sequence of the heavy chain of a pathological immunoglobulin G

1967 ◽  
Vol 104 (2) ◽  
pp. 616-626 ◽  
Author(s):  
PJ Piggot ◽  
EM Press
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Partial Sequence

scholarly journals Allotype-related sequence variation of the heavy chain of rabbit immunoglobulin G

1968 ◽  
Vol 107 (6) ◽  
pp. 753-763 ◽  
Author(s):  
J. W. Prahl ◽  
R R Porter
Keyword(s):  
Amino Acid ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Amino Acid Residues ◽  
Related Sequence ◽  
Heavy Chains ◽  
Methionine Residue ◽  
Isolation And Characterization ◽  
Rabbit Immunoglobulin

The heavy chain of rabbit immunoglobulin G exists in three major allotypic patterns, Aa1–Aa3. A comparison of the amino acid compositions of the heavy chains isolated from immunoglobulin IgG homozygous for each allotypic determinant revealed the presence of an additional methionine residue per chain in the Aa3 allotype relative to the Aa1 and Aa2 allotypes. The position of the additional methionine residue was determined by cyanogen bromide cleavage and by tryptic digestion of the γ-chains; it coincided with the inter-Fd–Fc area of the chain. Isolation and characterization of the corresponding tryptic peptides of 31 amino acid residues from each of the allotypes showed the presence of a methionine-for-threonine replacement in the Aa3 allotype, but only in about 70–80% of the molecules. No other allotypic variations were seen in this tryptic peptide. Allotypically related variations in composition were also detected in the N-terminal cyanogen bromide-cleavage peptide.

scholarly journals The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes

1967 ◽  
Vol 105 (3) ◽  
pp. 1019-1028 ◽  
Author(s):  
J. W. Prahl
Keyword(s):  
Gene Duplication ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Disease Protein ◽  
Heavy Chain Disease

The sequences of the C-terminal octadecapeptides obtained by cyanogen bromide cleavage of the γ-chains of myeloma proteins of the four subclasses, and a urinary heavy-chain-disease protein, have been determined. Although the sequences were markedly homologous, unique replacements were identified that distinguished between the γ2b, γ2c and γ2d subclasses. The data are in accord with the postulated existence of four genetic loci or cistrons, these having arisen by the process of gene duplication.

Structure of heavy chain from strain 13 guinea pig immunoglobulin-G(2). I. Isolation of cyanogen bromide fragments

Biochemistry ◽  
1971 ◽  
Vol 10 (1) ◽  
pp. 1-8 ◽  
Author(s):  
John J. Cebra ◽  
Keven J. Turner ◽  
Barbara K. Birshtein
Keyword(s):  
Guinea Pig ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide

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

1969 ◽  
Vol 112 (2) ◽  
pp. 173-185 ◽  
Author(s):  
J. M. Wilkinson
Keyword(s):  
Amino Acids ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Terminal Sequence ◽  
Heavy Chains ◽  
Terminal Fragment ◽  
Rabbit Immunoglobulin

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.

scholarly journals Common peptides from the N-terminal half of heavy chain of immunoglobulin G from normal rabbit serum and a specific antibody

1968 ◽  
Vol 107 (1) ◽  
pp. 69-77 ◽  
Author(s):  
J. J. Cebra ◽  
D. Givol ◽  
R R Porter
Keyword(s):  
Heavy Chain ◽  
Specific Antibody ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Tryptic Digestion ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Specific Antibodies ◽  
Comparative Sequence ◽  
Lysine Residues

Fragment C-1, the N-terminal half of the heavy chain of rabbit immunoglobulin G, was prepared by cyanogen bromide cleavage from the heavy chain of immunoglobulin G obtained both from the pooled serum of normal rabbits and from specific anti-dinitrophenyl antibody. Tryptic digestion of fragment C-1 after the lysine residues had been allowed to react with S-ethyl trifluorothioacetate led to the isolation of six peptides from inert immunoglobulin G and specific antibody that appear to account for most of this section of the heavy chain. This approach should make possible comparative sequence studies of the Fd section of the heavy chain from different allotypes and from specific antibodies.

Structure of the heavy chain from strain 13 guinea pig immunoglobulin G1: isolation of cyanogen bromide fragments

Biochemistry ◽  
1976 ◽  
Vol 15 (3) ◽  
pp. 624-629 ◽  
Author(s):  
Daniel E. Tracey ◽  
Sammy H. Liu ◽  
John J. Cebra
Keyword(s):  
Guinea Pig ◽  
Heavy Chain ◽  
Cyanogen Bromide

scholarly journals Differential reduction of interchain disulphide bonds of mouse immunoglobulin G

1968 ◽  
Vol 107 (6) ◽  
pp. 823-828 ◽  
Author(s):  
Alan R. Williamson ◽  
Brigitte A. Askonas
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Polyacrylamide Gel Electrophoresis ◽  
Partial Reduction ◽  
Free Light Chains ◽  
Myeloma Protein ◽  
Heavy Chains ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Mouse Immunoglobulin

The relative lability of the interchain disulphide bonds of mouse G2a-myeloma protein 5563 was studied as a function of 2-mercaptoethanol concentration. Analysis of partial-reduction mixtures by polyacrylamide-gel electrophoresis and microdensitometry showed that the disulphide bonds between light and heavy chains are much more susceptible to reduction than the bonds between heavy chains. At a low concentration of 2-mercaptoethanol (10mm) the major dissociable products of mouse immunoglobulin G are heavy-chain dimers and free light chains. These findings contrast with the reported behaviour of rabbit immunoglobulin G, for which the lability of inter-heavy-chain bonds was found to exceed that of the bonds linking light and heavy chains (Hong & Nisonoff, 1965); the relative stability of rabbit immunoglobulin G interchain bonds was confirmed in the present study. Examination of human immunoglobulin G and an immunoglobulin G (γ2) of guinea pig showed that at least in the majority of molecules, as with mouse immunoglobulin G, the disulphide bonds between light and heavy chains are more susceptible to reduction than the inter-heavy-chain bonds.

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