Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties.

N Cimerman, M D Kosorok, B D Korant, B Turk, V Turk
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引用次数: 21

Abstract

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.

牛腮腺胱抑素C的特性:半胱氨酸蛋白酶抑制和抗病毒特性。
半胱氨酸蛋白酶抑制剂Cystatin C是一种低Mr半胱氨酸蛋白酶抑制剂,经匀浆碱性处理、亲和层析、凝胶过滤和离子交换层析从牛腮腺中分离得到。纯化后的抑制剂的pl为8.0,Mr为14500。该抑制剂的n端序列和氨基酸组成证实其与牛初乳胱抑素C同源。胱抑素C快速抑制木瓜蛋白酶(kass = 5.5 × 10(7) M-1s-1),并紧密抑制木瓜蛋白酶(Ki = 0.02 nM),而与牛组织蛋白酶B的相互作用则弱得多(Ki = 4.4 nM)。牛胱抑素C对脊髓灰质炎病毒感染的人Hela细胞也显示出微弱的抗病毒作用。
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