Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168-Reference-Cited by-同舟云学术

Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168

Published:1991-03 Issue:5 Volume:173 Page:1824-1826
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Sugahara T¹,Konno Y¹,Ohta H¹,Ito K¹,Kaneko J¹,Kamio Y¹,Izaki K¹

Affiliation:

1. Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.

Abstract

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, Km, pH stability, and peptide maps.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.173.5.1824-1826.1991

Reference11 articles.

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4. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis;Hedck J. L.;Arch. Biochem. Biophys.,1968

5. Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis;Hulit F. M.;J. Bacteriol.,1990

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