Juliani M H, Da Costa Maia J C
Biochim Biophys Acta. 1979 Apr 12;567(2):347-56. doi: 10.1016/0005-2744(79)90121-9.
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.
在水霉艾美球囊霉的游动孢子提取物中已鉴定出蛋白激酶(ATP:蛋白质磷酸转移酶,EC 2.7.1.37)和环腺苷3',5'-单磷酸结合活性。这些活性的75%以上存在于可溶部分。可溶蛋白激酶活性通过DEAE-纤维素色谱法分离为三个峰(I、II和III)。峰I依赖于酪蛋白且对环磷酸腺苷不敏感。峰II依赖于组蛋白且不依赖于环磷酸腺苷;该酶被来自牛肌肉的热稳定抑制剂抑制。峰III以组蛋白为底物并被环磷酸腺苷激活。