scholarly journals Sequence studies on the heavy chain of rabbit immunoglobulin A of different a-locus allotypes

1977 ◽  
Vol 167 (1) ◽  
pp. 255-267 ◽  
Author(s):  
A P Johnstone ◽  
L E Mole

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.

1974 ◽  
Vol 143 (3) ◽  
pp. 723-732 ◽  
Author(s):  
Jean-Claude Jaton

The amino acid sequence between residues 70 and 116 of the V (variable) region of the H (heavy) chain derived from rabbit antibody BS-5, specific for type III pneumococcal polysaccharide, was determined. The sequence of this section of the H chain which includes the hypervariable residues 94 to about 112 was unique, although minor variant sequences present in the H chain preparation would not have been detected by the techniques used in this work. Taken together with the known sequences of the N-terminal 69 residues of H chain BS-5 (Jaton & Braun, 1972) and of the V region of the light chain (Jaton, 1974b), the data establish the complete sequence of the V domain of a rabbit immunoglobulin G. The V region of H chain BS-5 is compared with the basic sequences of the three human V region subgroups known to date, with one mouse H chain, and with guinea-pig pooled H chains. Even though chains from guinea pig and mouse clearly belong to the subgroup III of variability (VHIII), rabbit H chain BS-5 (allotypic variant a1) appears more closely related to the subgroup VHII than to the subgroups VHIII or VHI. The homology between VL and VH regions of antibody BS-5 (28%) is not greater than that observed between the VH region of antibody BS-5 and the VL regions of different rabbit antibodies.


1970 ◽  
Vol 116 (2) ◽  
pp. 249-259 ◽  
Author(s):  
R. G. Fruchter ◽  
S. A. Jackson ◽  
L. E. Mole ◽  
R. R. Porter

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.


1968 ◽  
Vol 107 (1) ◽  
pp. 79-88 ◽  
Author(s):  
J. J. Cebra ◽  
L. A. Steiner ◽  
R R Porter

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.


Biochemistry ◽  
1979 ◽  
Vol 18 (19) ◽  
pp. 4068-4080 ◽  
Author(s):  
Lisa A. Steiner ◽  
Angeles Garcia-Pardo ◽  
Michael N. Margolies

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