Immunoglobulin M and Secretory Immunoglobulin A: Presence of a Common Polypeptide Chain Different from Light Chains
Authors:
- 19 March 1971
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 171 (3976) , 1163-1165
Abstract
Unique polypeptide chains have been isolated from S -sulfonated light-chain fractions of human serum immunoglobulin M and colostral immunoglobulin A. Their electrophoretic mobilities, molecular weights, peptide maps, amino acid compositions, and antigenic determinants are very similar or perhaps identical but differ from those of light chains and secretory piece.Keywords
This publication has 12 references indexed in Scilit:
- Novel Subunit in Secretory IgANature, 1970
- Studies on the structural variation of the H chain of immunoglobulin M(IgM)Archives of Biochemistry and Biophysics, 1969
- Secretory Immunoglobulins1968
- Polypeptide Chain Structure of Rabbit Immunoglobulins. III. Secretory γA-Immunoglobulin from Colostrum*Biochemistry, 1967
- [36] Paper chromatography and electrophoresis; special procedure for peptide maps1967
- [19] Performic acid oxidation1967
- Electrophoretic Heterogeneity of Polypeptide Chains of Specific AntibodiesScience, 1966
- Reduction and Proteolytic Degradation of Immunoglobulin A from Human Colostrum.Acta Chemica Scandinavica, 1966
- Limited cleavage of disulphide bonds of pig gamma-globulin by S-sulphonationCollection of Czechoslovak Chemical Communications, 1964
- On the Determination of Cystine as Cysteic AcidJournal of Biological Chemistry, 1963