| Literature DB >> 3084949 |
Y Fujiyama, M Iwaki, K Hodohara, S Hosoda, K Kobayashi.
Abstract
Fc fragments of human immunoglobulin A(IgA) of IgA1 subclass and IgA2 subclass of A2m(1) allotype were prepared from IgA paraproteins by digestion with a protease from Clostridium sp. (M.O.-6). The N-terminal tetrapeptide of Val-Pro-Ser-Thr- for the Fc of IgA1 subclass, and that of Val-Pro-Pro-Pro- for the Fc of IgA2:A2m(1) allotype, were identified by sequence analysis. The site of cleavage by the protease was defined to be at the Pro-Val peptide bond, which is a common peptide bond present at 221-222 in both alpha chains. IgA of IgA2 subclass of A2m(2) allotype is resistant to the protease due to the different, Arg-Val, peptide bond at the same position.Entities:
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Year: 1986 PMID: 3084949 DOI: 10.1016/0161-5890(86)90036-2
Source DB: PubMed Journal: Mol Immunol ISSN: 0161-5890 Impact factor: 4.407