Characterization of Cystatin C from Bovine Parotid Glands: Cysteine Proteinase Inhibition and Antiviral Properties

• Published in: Biological Chemistry Vol. 377; no. 1; pp. 19 - 24
• Main Authors: Cimerman, Nina, Drobnič Košorok, Marinka, Korant, Bruce D., Turk, Boris, Turk, Vito
• Format: Journal Article
• Language: English
• Published: Berlin, New York Walter de Gruyter, Berlin / New York 1996; De Gruyter
• Subjects: Amino Acid Sequence; Animals; Antiviral Agents - pharmacology; Cattle; Cystatin C; Cystatins - chemistry; Cystatins - isolation & purification; Cystatins - pharmacology; Cysteine Proteinase Inhibitors - pharmacology; Cytopathogenic Effect, Viral - drug effects; Humans; Kinetics; Molecular Sequence Data; Molecular Weight; Parotid Gland - chemistry; Poliovirus - drug effects; Viral Plaque Assay
• ISSN: 0177-3593; 1437-4315
• DOI: 10.1515/bchm3.1996.377.1.19

Cystatin C, a low Mr cysteine proteinase inhibitor was isolated from bovine parotid glands by a procedure which includes alkaline treatment of the homogenate, affinity chromatography, gel filtration and ion exchange chromatography. The purified inhibitor has a pl of 8.0 and Mr of 14500. The identity with bovine cystatin C from colostrum was confirmed by N-terminal sequence of the inhibitor and amino acid composition. Cystatin C rapidly (kass = 5.5 x 10(7) M-1s-1) and tightly inhibits papain (Ki = 0.02 nM), whereas its interaction with bovine cathepsin B is substantially weaker (Ki = 4.4 nM). Bovine cystatin C also shows a weak antiviral effect on poliovirus infected human Hela cells.