Preparation of an active Fd fragment by cyanogen bromide cleavage of an IgG heavy chain from a homogeneous rabbit antibody

1978 ◽  
Vol 15 (12) ◽  
pp. 937-940 ◽  
Author(s):  
P.H. Ehrlich ◽  
G.R. Matsueda ◽  
M.N. Margolies ◽  
E. Haber
Keyword(s):  
Heavy Chain ◽  
Cyanogen Bromide ◽  
Rabbit Antibody

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 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 Affinity labelling of the binding site of rabbit antibody. Evidence for the involvement of the hypervariable regions of the heavy chain

1974 ◽  
Vol 139 (1) ◽  
pp. 135-149 ◽  
Author(s):  
Christopher E. Fisher ◽  
Elizabeth M. Press
Keyword(s):  
Binding Site ◽  
Heavy Chain ◽  
Binding Sites ◽  
Light Chains ◽  
Rabbit Antibody ◽  
Heavy Chains ◽  
Group 4 ◽  
Hypervariable Regions ◽  
Affinity Labelling ◽  
Antibody Complex

The binding sites of rabbit antibodies with affinity for the haptenic group 4-azido-2-nitrophenyl-lysine have been specifically labelled by photolysis of the hapten–antibody complex. The extent of covalent labelling was 0.5–0.9mol of hapten bound/mol of antibody and, by using an immunoadsorbent, antibody with 1.3mol of hapten/mol was obtained. The antibody was specifically labelled in the binding site and the ratio of labelling of heavy and light chains was in the range 3.3–5.0. The labelled heavy chains were cleaved by CNBr treatment and after reduction and alkylation of the intrachain bonds, were digested with trypsin. Evidence is presented that two regions of the heavy chain, positions 29–34 and 95–114, together contain about 80% of the label on the heavy chain; these two regions respectively include two of the hypervariable regions of rabbit heavy chain.

scholarly journals Completion of the analysis of the primary structure of the variable domain of a homogeneous rabbit antibody to type III pneumococcal polysaccharide

1974 ◽  
Vol 143 (3) ◽  
pp. 723-732 ◽  
Author(s):  
Jean-Claude Jaton
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Guinea Pig ◽  
Heavy Chain ◽  
Variable Region ◽  
Complete Sequence ◽  
Rabbit Antibody ◽  
Type Iii ◽  
Minor Variant ◽  
V Region

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.

scholarly journals Partial amino acid sequence in the N-terminal region of an anti-pneumococcal immunoglobulin heavy chain of allotype a2

1974 ◽  
Vol 139 (1) ◽  
pp. 281-283 ◽  
Author(s):  
Jean-Claude Jaton ◽  
Joseph Haimovich
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Sequence Variability ◽  
Rabbit Antibody ◽  
Partial Amino Acid Sequence ◽  
Heavy Chains

The amino acid sequence of the N-terminal 48 residues of the heavy chain derived from a homogeneous rabbit antibody to type III pneumococci is described. This chain of allotype a2 is compared with other rabbit heavy chains of allotypes a1, a2 and a3. Within the N-terminal 25 positions, two chains which carry the same allotype a2 possess identical amino acid sequences, but differ markedly from heavy chains of allotypes a1 and a3. Sequence variability is observed in residues 26–27 and 30–34, but not in residues 35–48.

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