Primary structure of a new cysteine proteinase inhibitor from pig leucocytes.
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.
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Department of Biochemistry, J. Stefan Institute, Ljubljana, Yugoslavia.
Kopitar
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Jerala
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Turk
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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
D015853:Cysteine Proteinase Inhibitors