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The complete primary structure of abrin‐a B chain
Author(s) -
Chen Yung-Liang,
Chow Lu-Ping,
Tsugita Akira,
Lin Jung-Yaw
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81076-x
Subject(s) - thermolysin , chemistry , peptide sequence , chymotrypsin , trypsin , biochemistry , protein primary structure , ricin , protease , amino acid , enzyme , toxin , gene
The complete 267 amino acid sequence of abrin‐a B chain was determined by analysis of peptides obtained by digestion with trypsin, chymotrypsin, lysyl endopeptidase, Staphylacaccus aureus V8 protease and thermolysin. The sequence is not identical with that predicted previously by nucleotide sequencing, indicating the presence of isoforms of abrin. Comparison of the amino acid sequence of abrin‐a B chain with that of ricin‐D B chain reveals a high degree of sequence identity (59%). Abrin‐a B chain appears to consist of two domains, each domain with subdomains (α, β, γ) of about 40 amino acid residues.