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
收藏
页码：1824 / 1826
页数：3
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