Premium
Primary structure of a new cysteine proteinase inhibitor from pig leucocytes
Author(s) -
Ritonja Anka,
Kopitar Majda,
Jerala Roman,
Turk Vito
Publication year - 1989
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(89)81093-2
Subject(s) - cysteine , proteinase inhibitor , cysteine proteinase inhibitors , chemistry , protein primary structure , biochemistry , serine proteinase inhibitors , primary (astronomy) , microbiology and biotechnology , biology , peptide sequence , enzyme , gene , apoptosis , protease , programmed cell death , caspase , serine protease , physics , astronomy
The primary structure of a pig leucocyte cysteine proteinase inhibitor, also called cathelin, was determined. The sequence was obtained from analyses of peptides isolated from the chymotryptic, endoproteinase Lys‐C and protease V8 digests, and by analysis of the peptides derived from the hydrolysis of the aspartyl‐prolyl bond of the carboxymethylated inhibitor. The inhibitor consists of 96 residues. The N‐terminal residue of the inhibitor is pyrrolidonecarboxylic acid. The amino acid sequence of cathelin suggests the appearance of a new family of cysteine proteinase inhibitors.