PURIFICATION AND PROPERTIES OF SECRETORY ASPARTIC PROTEINASE FROM CANDIDA ALBICANS
- VernacularTitle:白色念珠菌分泌型天冬氨酸蛋白酶的纯化与性质
- Author:
Dan-Min WANG
;
Li-Yin LIU
;
Lu YE
;
Lei GAO
;
- Publication Type:Journal Article
- Keywords:
Secretory aspartic proteinase, Purification, Property
- From:
Microbiology
1992;0(02):-
- CountryChina
- Language:Chinese
-
Abstract:
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.
