PARTIAL-PURIFICATION AND BIOCHEMICAL-PROPERTIES OF ACID AND ALKALINE-PHOSPHATASES FROM MYXOCOCCUS-CORALLOIDES-D

被引：42

作者：

GONZALEZ, F ^{[1
]}

FAREZVIDAL, ME ^{[1
]}

ARIAS, JM ^{[1
]}

MONTOYA, E ^{[1
]}

机构：

[1] UNIV GRANADA,FAC CIENCIAS,DEPT MICROBIOL,E-18071 GRANADA,SPAIN

来源：

JOURNAL OF APPLIED BACTERIOLOGY | 1994年 / 77卷 / 05期

关键词：

D O I：

10.1111/j.1365-2672.1994.tb04403.x

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Acid phosphatase and alkaline phosphatase from vegetative cells of Myxococcus coralloides D were purified by two chromatographic steps. The molecular weights were estimated by gel filtration and SDS-PAGE. Optimum pH, stability, optimum temperature and thermal inactivation studies were made for both enzymes. EDTA and other chelating agents inhibited alkaline but not acid activity. Mg2+ activated the alkaline phosphatase, while the acid phosphatase was inhibited by fluoride. Both enzymes degraded a number of phosphomonoesters, but were unable to hydrolyse either polyphosphates or cAMP. The K-m, values of the acid and alkaline phosphatases for p-nitrophenylphosphate were 5.0 x 10(-3) mol l(-1) and 1.5 x 10(-3) mol l(-1), respectively.

引用

页码：567 / 573

页数：7

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