Primary structure of a new cysteine proteinase inhibitor from pig leucocytes

作者：Anka Ritonja, Majda Kopitar, Roman Jerala, Vito Türk · 发表于：FEBS Letters · 年份：1989 · DOI：10.1016/0014-5793(89)81093-2 · 被引用次数：151 · 研究领域：Biochemical and Structural Characterization、Chemical Synthesis and Analysis、Protein Hydrolysis and Bioactive Peptides

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 pyrrolidone-carboxylic acid. The amino acid sequence of cathelin suggests the appearance of a new family of cysteine proteinase inhibitors.