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肝片吸虫:一种分泌的组织蛋白酶L样蛋白酶可切割宿主免疫球蛋白。

Fasciola hepatica: a secreted cathepsin L-like proteinase cleaves host immunoglobulin.

作者信息

Smith A M, Dowd A J, Heffernan M, Robertson C D, Dalton J P

机构信息

School of Biological Sciences, Dublin City University, Republic of Ireland.

出版信息

Int J Parasitol. 1993 Dec;23(8):977-83. doi: 10.1016/0020-7519(93)90117-h.

Abstract

Adult Fasciola hepatica secrete a cysteine proteinase capable of cleaving host IgG close to the papain cleaving site. The proteinase was separated by size permeation chromatography. Gelatin-substrate polyacrylamide gel electrophoresis analysis revealed that the proteinase migrates as 6 proteolytic bands in the apparent molecular size range 60-90 kDa. Based on pH profiles of activity, inhibition studies using diethylpyrocarbonate and the diazomethylketone Z-phe-ala-CHN2, and characterising the substrate specificity of the enzymes using fluorogenic peptide substrates we have shown that the 60-90-kDa proteinases are cathepsin L-like proteinases.

摘要

成年肝片吸虫分泌一种半胱氨酸蛋白酶,该酶能够在靠近木瓜蛋白酶切割位点处裂解宿主免疫球蛋白G(IgG)。通过尺寸排阻色谱法分离该蛋白酶。明胶底物聚丙烯酰胺凝胶电泳分析显示,该蛋白酶以6条蛋白水解带的形式迁移,表观分子大小范围为60 - 90 kDa。基于活性的pH谱、使用焦碳酸二乙酯和重氮甲基酮Z-苯丙氨酸-丙氨酸-CHN2的抑制研究,以及使用荧光肽底物表征酶的底物特异性,我们已表明60 - 90 kDa的蛋白酶是组织蛋白酶L样蛋白酶。

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