Amino Acid Sequence Similarities in Two Human Anti Gamma Globulin Antibodies | Zendy

J. Donald Capra | Zendy; Henry G. Kunkel | Zendy

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Amino Acid Sequence Similarities in Two Human Anti Gamma Globulin Antibodies

Author(s) -

J. Donald Capra,

Henry G. Kunkel

Publication year - 1970

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.67.1.87

Subject(s) - gamma globulin , antibody , peptide sequence , immunoglobulin light chain , amino acid , sequence (biology) , biology , amino acid residue , globulin , biochemistry , chemistry , microbiology and biotechnology , genetics , immunology , gene

Certain individuals with hypergammaglobulinemic purpura contain in their serum anti gamma globulins of restricted heterogeneity. These antibodies, characteristically of the gammaG type, were isolated from two unrelated individuals and their light polypeptide chains were subjected to amino acid sequence analysis. Although these anti gamma globulin antibodies conform to the basic VK(1) sequence, substitutions not previously encountered were found in five positions. The two antibodies were identical with each other up to residue 40 from the N-terminus of the light chains.

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