Literature DB >> 194626

[Detection of multiple forms of polyphosphate phosphohydrolase from Endomyces magnusii].

T P Afanas'eva, S O Uryson, I S Kulaev.   

Abstract

Labile polyphosphate phosphohydrolase from Endomyces magnusii is 27-fold purified by means of fractionation with ammonium sulphate, gel filtration on Sephadex G-75 and Biogel P-60 and chromatography on DEAE cellulose. Chromatography on DEAE Sephadex A-50, isoelelctric focusing and polyacrylamide gel electrophoresis of the enzyme preparation revealed 3 different fractions with polyphosphate phosphohydrolase activity (PPPH1, PPPH2 and PPPH3). Relative content of these fractions in E. magnusii cells is 30%, 55% and 15% respectively. Isoelectric points are: PPPH1--pH 5.1--5.2; PPPH2--pH 6.0--6.1; PPPH3--pH 6.3--6.4. PPPH1 and PPPH2 are found to be the most labile. PPPH3 is more stable under isolation procedure and storage. The fractions have similar molecular weight (48 000 +/- 3000).

Entities:  

Mesh:

Substances:

Year:  1976        PMID: 194626

Source DB:  PubMed          Journal:  Biokhimiia        ISSN: 0320-9725


  2 in total

1.  Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. I. Phosphatases and ATP-glucokinase.

Authors:  L V Trilisenko; J Novotná; V Erban; V Bĕhal; Z Hostálek; I S Kulaev
Journal:  Folia Microbiol (Praha)       Date:  1987       Impact factor: 2.099

2.  Properties of polyphosphatase of Acinetobacter johnsonii 210A.

Authors:  C F Bonting; G J Kortstee; A J Zehnder
Journal:  Antonie Van Leeuwenhoek       Date:  1993       Impact factor: 2.271

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.