| Literature DB >> 221023 |
M H Juliani, J C Da Costa Maia.
Abstract
Protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) and cyclic adenosine 3',5'-monophosphate binding activities have been identified in zoospore extracts of the water mold Blastocladiella emersonii. More than 75% of these activities is found in the soluble fraction. Soluble protein kinase activity is resolved in three peaks(I, II and III) by DEAE-cellulose chromatography. Peak I is casein dependent and insensitive to cyclic AMP. Peak II is histone dependent and cyclic AMP independent; this enzyme is inhibited by the heat-stable inhibitor from bovine muscle. Peak III utilizes histone as substrate and is activated by cyclic AMP.Entities:
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Year: 1979 PMID： 221023 DOI： 10.1016/0005-2744(79)90121-9
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002