Amino acid sequence of the heavy-chain variable region of the crystallizable human myeloma protein Dob

Biochemistry ◽  
1979 ◽  
Vol 18 (19) ◽  
pp. 4068-4080 ◽  
Author(s):  
Lisa A. Steiner ◽  
Angeles Garcia-Pardo ◽  
Michael N. Margolies
Biochemistry ◽  
1977 ◽  
Vol 16 (6) ◽  
pp. 1170-1175 ◽  
Author(s):  
Mark Vrana ◽  
Stuart Rudikoff ◽  
Michael Potter

1991 ◽  
Vol 372 (2) ◽  
pp. 795-818 ◽  
Author(s):  
R. Joachim FRIEDRICH ◽  
Rolf BÄTGE ◽  
Iris SCHRANNER ◽  
Ulrike KOTUCHA ◽  
Klaus ECKART ◽  
...  

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 117 (4) ◽  
pp. 641-660 ◽  
Author(s):  
E. M. Press ◽  
N. M. Hogg

The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another γ 1 chain, Eu, a μ chain, Ou, and the partial sequence of a fourth γ 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the γ 1 chains, Cor.


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