PURIFICATION AND PROPERTIES OF 2 MEMBRANE ALKALINE-PHOSPHATASES FROM BACILLUS-SUBTILIS-168

被引：8

作者：

SUGAHARA, T ^{[1
]}

KONNO, Y ^{[1
]}

OHTA, H ^{[1
]}

ITO, K ^{[1
]}

KANEKO, J ^{[1
]}

KAMIO, Y ^{[1
]}

IZAKI, K ^{[1
]}

机构：

[1] TOHOKU UNIV, FAC AGR, DEPT AGR CHEM, SENDAI 981, JAPAN

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 05期

关键词：

D O I：

10.1128/jb.173.5.1824-1826.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Two alkaline phosphatases were extracted from the membranes of Bacillus subtilis 168 stationary-phase cells and purified as homogeneous proteins by hydroxyapatite column chromatography. Alkaline phosphatases I and II differed in several properties such as subunit molecular weight, substrate specificity, thermostability, K(m), pH stability, and peptide maps.

引用

页码：1824 / 1826

页数：3

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