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白色念珠菌分泌型天冬氨酸蛋白酶的纯化与性质 被引量:4

PURIFICATION AND PROPERTIES OF SECRETORY ASPARTIC PROTEINASE FROM CANDIDA ALBICANS
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摘要 利用硫酸铵分级沉淀和DEAE-Sephacel离子交换层析从白色念珠菌WD27培养液中提纯得到一种蛋白酶,纯化倍数为25.4,收率为5.2%。其活性可被抑胃肽特异抑制,初步鉴定该酶为天冬氨酸蛋白酶。该酶在酸性范围内有水解蛋白活性,最适作用pH为4.0,最适温度为37℃。酶在pH5.0~6.0、45℃以下较稳定,该酶具有较广的底物作用范围,对牛血红蛋白最敏感。酶作用于牛血红蛋白的米氏常数Km为0.814mmol/L。 An extracellular proteinase from Candida albicans WD27 was purified by (NH4)2SO4 fractionation and DEAE-Sephacel ion-exchange chromatography with 25.4 fold and 5.2% yield. This enzyme appeared to be aspartic proteinase since the enzyme activity could be inhibited by pepstatin which was specific inhibitor of this class of proteinase. The enzyme had an acidic proteolytic activity profile with the optimum pH of 4.0. The optimum temperature of the enzyme activity was 37℃. The proteinase had a broad substrate specificity with the highest susceptibility to bovine hemoglobin. The Km for bovine hemoglobin was determined to be 0.814mmol/L.
出处 《微生物学通报》 CAS CSCD 北大核心 2002年第2期27-30,共4页 Microbiology China
关键词 分泌型天冬氨酸蛋白酶 致病性 毒力因子 白色念珠菌 纯化 性质 Secretory aspartic proteinase, Purification, Property
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  • 1Kwon Chung Kf,Infect Immun,1985年,49卷,571页 被引量:1

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