Literature DB >> 718947

Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization.

S D Schaffel, F M Hulett.   

Abstract

The membrane-associated alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from Bacillus licheniformis MC14, a facultative thermophile, was purified to homogeneity in buffer containing 0.2 M Mg2+. The alkaline phosphatase purified in this manner is insoluble upon removal of the magnesium by dialysis. This insoluble alkaline phosphatase has been characterized and compared to the previously purified heat-solubilized enzyme (Hulett-Cowling, F.M. and Campbell, L.L. (1971) Biochemistry 10, 1364--1371).

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Year:  1978        PMID: 718947     DOI: 10.1016/0005-2744(78)90137-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis.

Authors:  F M Hulett; C Bookstein; K Jensen
Journal:  J Bacteriol       Date:  1990-02       Impact factor: 3.490

2.  Cloning and characterization of the Bacillus licheniformis gene coding for alkaline phosphatase.

Authors:  F M Hulett
Journal:  J Bacteriol       Date:  1984-06       Impact factor: 3.490

3.  Production of two extracellular alkaline phosphatases by a psychrophilic arthrobacter strain.

Authors:  P de Prada; J Loveland-Curtze; J E Brenchley
Journal:  Appl Environ Microbiol       Date:  1996-10       Impact factor: 4.792

4.  Two alkaline phosphatase genes positioned in tandem in Bacillus licheniformis MC14 require different RNA polymerase holoenzymes for transcription.

Authors:  F M Hulett; P Z Wang; M Sussman; J W Lee
Journal:  Proc Natl Acad Sci U S A       Date:  1985-02       Impact factor: 11.205

5.  Lactoperoxidase-125I localization of salt-extractable alkaline phosphatase on the cytoplasmic membrane of Bacillus licheniformis.

Authors:  D B Spencer; F M Hulett
Journal:  J Bacteriol       Date:  1981-02       Impact factor: 3.490

  5 in total

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