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

1971 ◽  
Vol 124 (2) ◽  
pp. 301-318 ◽  
Author(s):  
L. E. Mole ◽  
S. A. Jackson ◽  
R. R. Porter ◽  
J. M. Wilkinson
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Sequence Variation ◽  
Variable Region ◽  
Related Sequence ◽  
Heavy Chains ◽  
Rabbit Immunoglobulin ◽  
Variable Section ◽  
Terminal Section ◽  
Constant Section

The sequence has been completed of the N-terminal 94 residues of the variable section of the Fd fragment of heavy chains from rabbit immunoglobulin G (IgG) of allotype As1. Most of the sequence of the same section from IgG of allotype Aa3 is also reported. These results, in conjunction with a substantial sequence of the variable region of allotype Aa2 reported elsewhere (Fleischman, 1971), show the presence of 16 positions (including six consecutive positions) in which the residue present correlates with the allotype. No allotype-related sequence variation has been found in the constant section of the Fd fragment. This evidence supports the view that two genes code for the heavy chain and it can be used as evidence in favour of somatic mutation as the origin of the variability in the sequence of the N-terminal section. The evolutionary origin of the ‘a’ locus allotypes of rabbit immunoglobulins remains obscure.

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 partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G

1968 ◽  
Vol 107 (1) ◽  
pp. 79-88 ◽  
Author(s):  
J. J. Cebra ◽  
L. A. Steiner ◽  
R R Porter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Preceding Paper ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Heavy Chains ◽  
Rabbit Immunoglobulin ◽  
Terminal Section

The partial amino acid sequence of two large peptides is described. These were prepared from the N-terminal half of the heavy chain of immunoglobulin G from pooled normal rabbit serum by tryptic digestion after the ∈-amino groups of the lysine residues had been blocked with S-ethyl trifluorothioacetate. These peptides are believed to account for about 145 residues of fragment C-1, the N-terminal section of rabbit immunoglobulin G heavy chain prepared by cyanogen bromide cleavage. The evidence from the present paper and the preceding paper (Cebra, Givol & Porter, 1968) suggests that it may be possible to deduce a predominant amino acid sequence for most, if not all, of this section of the molecule.

scholarly journals Amino acid sequence of the N-terminal sixty-nine residues of heavy chain derived from a homogeneous rabbit antibody

1972 ◽  
Vol 130 (2) ◽  
pp. 539-546 ◽  
Author(s):  
Jean-Claude Jaton ◽  
D. G. Braun
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Heavy Chain ◽  
Sequence Variation ◽  
Sequence Variability ◽  
Rabbit Antibody ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Variable Section ◽  
Chain Sequence

The sequence of the N-terminal 69 residues of heavy chain from a homogeneous rabbit antibody to type III pneumococcal polysaccharide was determined. The sequence is similar to that found in heavy chains of normal pooled rabbit immunoglobulins of the same allotype Aa1. Two regions of the homogeneous heavy chain (residues 35–46 and 62–69) are very similar to corresponding regions of heavy chains from rabbit Aa2 immunoglobulin, as well as from mouse, guinea-pig and human immunoglobulins. In contrast, residues 47–62 appear to be variable. Comparison in this section with another homogeneous anti-pneumococcal antibody (Strosberg et al., 1972) of related specificity and of the same allotype indicates sequence variation in at least three positions. An antibody to group C streptococcal carbohydrate of allotype Aa2 (Fleischman, 1971) differs by five amino acids in the same region of the heavy chain. Sequence variability between these three antibodies does not occur in homologous positions within this variable section. Allotype-related sequences could not be identified in section 34–65.

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.

scholarly journals Sequence studies of the Fd section of the heavy chain of rabbit immunoglobulin G

1970 ◽  
Vol 116 (2) ◽  
pp. 249-259 ◽  
Author(s):  
R. G. Fruchter ◽  
S. A. Jackson ◽  
L. E. Mole ◽  
R. R. Porter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Partial Amino Acid Sequence ◽  
Limited Region ◽  
Heavy Chains ◽  
Total Sequence ◽  
Continuous Sequence ◽  
Rabbit Immunoglobulin

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.

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

1975 ◽  
Vol 151 (2) ◽  
pp. 337-349 ◽  
Author(s):  
D M Pratt ◽  
L E Mole
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Immunoglobulin G ◽  
Constant Region ◽  
Related Sequence ◽  
Variable Regions ◽  
Heavy Chains ◽  
Continuous Sequence ◽  
Rabbit Igg ◽  
Constant Section

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.

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 A genetic marker in the variable region of rabbit immunoglobulin heavy chain

1975 ◽  
Vol 151 (2) ◽  
pp. 351-359 ◽  
Author(s):  
L R Mole
Keyword(s):  
Genetic Marker ◽  
Heavy Chain ◽  
Variable Region ◽  
Immunoglobulin Heavy Chain ◽  
Heavy Chains ◽  
Rabbit Immunoglobulin ◽  
V Region ◽  
Peptide Map ◽  
Relationship Of ◽  
The Relationship

A previous study [Mole et al. (1971) Biochem. J. 124, 301-318] showed several differences in sequence between the variable (V) regions of rabbit immunoglobulin Aa1 and Aa3 heavy chains. The inheritance of one such difference has been followed in a family of 38 rabbits by a radioautographic peptide-‘map’ technique and is shown to segregate in a Mendelian fashion. This clearly demonstrates the presence of a genetic marker in the rabbit heavy-chain V region, although the finding that Aa2 and Aa3 heavy chains have identity of sequence in the region studied obscures the relationship of this genetic marker to the a locus.

scholarly journals The disulphide bonds of the heavy chain of rabbit immunoglobulin G

1970 ◽  
Vol 116 (2) ◽  
pp. 261-268 ◽  
Author(s):  
I. J. O'Donnell ◽  
B. Frangione ◽  
R. R. Porter
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Good Yield ◽  
Sequence Variants ◽  
Lower Yield ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Minor Sequence

Six peptides containing eight half-cystine residues were isolated in good yield, after either oxidation or reduction and carboxymethylation of fragment C-1, which contains the N-terminal half of the heavy chain of rabbit immunoglobulin G. The sequences of five of these peptides had been reported previously (Cebra, Steiner & Porter, 1968b; Wilkinson, 1969) and that of the sixth was established. Other peptides containing half-cystine residues were isolated in much lower yield and are presumed to be derived from minor sequence variants. The cystine-containing peptides from enzymic digests of whole immunoglobulin G and Fc fraction were studied by several techniques and the results obtained enable us to put forward a scheme of the arrangement of the inter- and intra-chain disulphide bonds.

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