Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. I. Phosphatases and ATP-glucokinase
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
2826319
DOI
10.1007/bf02887570
Knihovny.cz E-zdroje
- MeSH
- draslík farmakologie MeSH
- fosfatasy metabolismus MeSH
- glukokinasa metabolismus MeSH
- hořčík farmakologie MeSH
- kationty MeSH
- kinetika MeSH
- sodík farmakologie MeSH
- Streptomyces aureofaciens účinky léků enzymologie MeSH
- subcelulární frakce enzymologie MeSH
- thiokyanatany farmakologie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- benzyl thiocyanate MeSH Prohlížeč
- draslík MeSH
- fosfatasy MeSH
- glukokinasa MeSH
- hořčík MeSH
- kationty MeSH
- sodík MeSH
- thiokyanatany MeSH
Mycelia of a low- and a high-production strain of Streptomyces aureofaciens were converted into protoplasts and divided into five subcellular fractions in order to localize exopolyphosphatases (EC 3.6.1.11), triphosphatase (EC 3.6.1.25), inorganic diphosphatase (EC 3.6.1.1), apyrase (EC 3.6.1.5) and glucokinase (EC 2.7.1.2). The highest specific activity of enzymes hydrolyzing polyphosphates was found in cytoplasmic vesicles and membranes. Triphosphatase was detected in the periplasmic fraction. Periplasmic vesicles and cytoplasm exhibited a high activity of diphosphatase. Apyrase was found mainly in the fractions of membranes and cytoplasmic vesicles. Glucokinase was a cytoplasmic enzyme. The enzymes were released from membrane structures into cytoplasm or periplasmic space if benzyl thiocyanate (10 microM) was present in the growth medium.
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