title: Primary structure of a new cysteine proteinase inhibitor from pig leucocytes.
abstract: 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.
authors: Department of Biochemistry, J. Stefan Institute, Ljubljana, Yugoslavia.
authors: A
authors: A
authors: Ritonja
authors: M
authors: M
authors: Kopitar
authors: R
authors: R
authors: Jerala
authors: V
authors: V
authors: Turk
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015853:Cysteine Proteinase Inhibitors / Q000097:blood* / Q000302:isolation & purification; D007962:Leukocytes / Q000378:metabolism*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
chemical_list: D015853:Cysteine Proteinase Inhibitors