Protein kinase activities in cell-free extracts of Streptomyces coelicolor A3(2)
1989; Elsevier BV; Volume: 71; Issue: 9-10 Linguagem: Inglês
10.1016/0300-9084(89)90117-x
ISSN1638-6183
AutoresDeborah J. Stowe, Tony Atkinson, Nicholas H. Mann,
Tópico(s)Biochemical and Molecular Research
ResumoProtein kinase activities were detected in cell-free extracts of the B385 derivative of Streptomyces coelicolor A3(2); at least 12 polypeptides, ranging in Mr 6 000 to 98 000, were detectably phosphorylated, probably as O-monoesters, after incubation with gamma [32P]ATP. The culture stage of the mycelia used for production of the cell-free extracts determined the profile of phosphorylated polypeptides. Phosphoenol pyruvate acted as a potent modulator of the apparent degree of protein kinase activity. In addition Ca2+ ions, verapamil, chlorpromazine and anti-calmodulin antiserum had specific effects on the profile of phosphopolypeptides observed.
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