AN ALKALINE-PHOSPHATASE FROM THERMUS SP STRAIN-RT41A | Health & Environmental Research Online (HERO)

Health & Environmental Research Online (HERO)

Print Feedback Export to File

This record has one attached file:

Citation
Tags

HERO ID

1347203

Reference Type

Journal Article

Title

AN ALKALINE-PHOSPHATASE FROM THERMUS SP STRAIN-RT41A

Author(s)

Hartog, AT; Daniel, RM

Year

1992

Is Peer Reviewed?

Yes

Journal

International Journal of Biochemistry
ISSN: 0020-711X

Volume

Issue

Page Numbers

1657-1660

Web of Science Id

WOS:A1992JM70500016

Abstract

1. A thermostable orthophosphoric monoester phosphohydrolase (EC 3.1.3.1) from Thermus sp strain Rt41A has been purified 400-fold to give a specific activity of 25 U/mg at 60-degrees-C in 1M diethanolamine (pH 11.1). 2. The enzyme has a M(r) of 160,000 and is trimeric. 3 The half-life of the enzyme is 5 min at 85-degrees-C. 4. The enzyme has a wide specificity for a number of phosphate monoesters. 5. The K(m) of the enzyme is pH dependent, so the pH optimum of the enzyme is affected by the substrate concentration. 6. The enzyme is inhibited 50% by 20 mM Ca2+ or Mg2+. 7. The K(i) for phosphate, EDTA-di sodium salt and arsenate (in 1M diethanolamine, pH 11.1) is approx 1.2, 1.6 and 4 mM respectively. 8. Urea (200 mM) is not inhibitory.