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酿酒酵母胞内无机焦磷酸酶的分离纯化及性质
引用本文:苟萍 杨寿钧. 酿酒酵母胞内无机焦磷酸酶的分离纯化及性质[J]. 微生物学报, 1998, 38(3): 229-232
作者姓名:苟萍 杨寿钧
作者单位:新疆大学生物系 830046;中国科学院微生物研究所 100080
摘    要:An inorganic pyrophosphatase (EC3.6.1.1) from Saccharomyces cerevisiae was purified to PAGE homogeneity by sonication disruption. (NH4)2SO4 fractionation and DEAE-cellulose colunm chromatography. The optimum pH and temperature of the enzyme were 7.4~7. 8 and 60℃, respectively. The Km was 19.3 mmol / L. The enzyme required Mg2+ as a cofactor for hydrolysis of pyrophosphate and was inhibited by Ca2+, Hg2+, Pb2+, Mn2+.

关 键 词:酿酒酵母   无机焦磷酸酶   纯化与性质

PURIFICATION AND PROPERTIES OF INTERCELLULAR INORGANIC PYROPHOSPHTASE FROM SACCHAROMYCES CEREVISIAE
Gou Ping, Yang Shoujun. PURIFICATION AND PROPERTIES OF INTERCELLULAR INORGANIC PYROPHOSPHTASE FROM SACCHAROMYCES CEREVISIAE[J]. Acta microbiologica Sinica, 1998, 38(3): 229-232
Authors:Gou Ping   Yang Shoujun
Affiliation:Institute of Mirobiology, Chinese Academy of Sciences, Beijing 100080.
Abstract:An inorganic pyrophosphatase (EC3.6.1.1) from Saccharomyces cerevisiae was purified to PAGE homogeneity by sonication disruption, (NH4)2SO4 fractionation and DEAE-cellulose column chromatography. The optimum pH and temperature of the enzyme were 7.4-7.8 and 60 degrees C, respectively. The Km was 19.3 mmol/L. The enzyme required Mg2+ as a cofactor for hydrolysis of pyrophosphate and was inhibited by Ca2+, Hg2+, Pb2+, Mn2+.
Keywords:Saccharomyces cerevisiae   Inorganic pyrophosphatase   Purification and properties  
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