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.

scholarly journals Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment

1968 ◽  
Vol 106 (1) ◽  
pp. 15-21 ◽  
Author(s):  
B. Frangione ◽  
C. Milstein ◽  
Edward C. Franklin
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
The Other ◽  
Light Chains ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Other Hand ◽  
Terminal Loop ◽  
Heavy Chain Disease

The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present. The sequences appear to be identical in the Fc fragments of two types of chain studied (γ1 and γ3), and very similar to corresponding sequences of the Fc fragment in rabbit. These results suggest that the C-terminal half of the heavy chains is covalently folded (in a similar fashion to the light chains) with a C-terminal loop and an N-terminal loop. The similarity is emphasized by comparison of the sequence and location of the disulphide-bridged peptides of the C-terminal loop of heavy and light chains. The N-terminal loop, on the other hand, appears to be very different in Fc fragments and light chains. The C-terminal loop is the only one present in the F′c fragment.

Regulatory Genes controlling the Synthesis of Heavy Chains of Human Immunoglobulin-G

Nature ◽  
1967 ◽  
Vol 214 (5090) ◽  
pp. 783-785 ◽  
Author(s):  
NOELENE LOBB ◽  
C. C. CURTAIN ◽  
CHEV KIDSON
Keyword(s):  
Immunoglobulin G ◽  
Regulatory Genes ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G ◽  
Heavy Chains

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 Dynamics of Inter-heavy Chain Interactions in Human Immunoglobulin G (IgG) Subclasses Studied by Kinetic Fab Arm Exchange

2014 ◽  
Vol 289 (9) ◽  
pp. 6098-6109 ◽  
Author(s):  
Theo Rispens ◽  
Anna M. Davies ◽  
Pleuni Ooijevaar-de Heer ◽  
Samira Absalah ◽  
Onno Bende ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Igg Subclasses ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G

scholarly journals STRUCTURAL STUDIES OF HUMAN γG-MYELOMA PROTEINS OF DIFFERENT ANTIGENIC SUBGROUPS AND GENETIC SPECIFICITIES

1966 ◽  
Vol 124 (4) ◽  
pp. 715-732 ◽  
Author(s):  
B. Frangione ◽  
E. C. Franklin ◽  
H. H. Fudenberg ◽  
M. E. Koshland
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Heavy Chain ◽  
The Other ◽  
Structural Studies ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Methionine Sulfone ◽  
Peptide Maps ◽  
Heavy Chain Disease

1. Peptide maps of Fc fragments or heavy chains of 36 G myeloma proteins and two "heavy chain disease" proteins belonging to the four γ-chain subgroups revealed very striking similarities between them. However differences in a few peptides were noted. This was most pronounced for the Ge(γ2d) subgroup which lacked three peptides characteristic of the other three subgroups. While Fc fragments from different proteins belonging to the same subgroup appeared very similar, minor differences in addition to those based on currently recognized Gm factors were occasionally noted. 2. Fc fragments from Gm(a+) We(γ2b) proteins had a peptide previously shown to be characteristic of normal Gm(a+) γG-globulins. Fc fragments from Gm(a-) molecules belonging to the We(γ2b), Vi(γ2c), or Ne(γ2a) subgroups, whether Gm(b+), Gm(f+), or Gm(-), had the peptide previously identified in Gm(b+f+) normal γG-globulin. This "non-a" peptide was absent in peptide maps from Gm(-) molecules of the Ge(γ2d) subgroup which contained instead another peptide with the same electrophoretic mobility but migrating slightly further on chromatography. 3. Both the "a" and "non-a" peptides were pentapeptides having three amino acids in common, and differing in the other two. The "a" peptide contained one residue of lysine, aspartic acid, threonine, leucine, and glutamic acid. The "non-a" peptides prepared from Gm(b+), Gm(f+), and Gm(-) proteins were identical and contained one residue of lysine, threonine, and methionine sulfone, and two residues of glutamic acid. 4. Several possible mechanisms for the origin of these differences, and their possible role in serologic specificity are discussed.

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.

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