Silva A M, Gomes S L, Maia J C, Juliani M H
Departamento de Bioquimica, Universidade de São Paulo, Brasil.
Second Messengers Phosphoproteins. 1988;12(5-6):271-80.
Extracts of aggregation-competent cells of Dictyostelium discoideum have an S6 protein kinase activity which is inhibited in the presence of the inhibitor of the cAMP-dependent protein kinase. The phosphorylation of S6 is rapid, and decays rapidly. The S6 kinase activity is detectable in the 150,000g supernatant only in the presence of phosphatase inhibitors known for preserving the S6 kinase in other systems, indicating that the activated form of the enzyme is phosphorylated by the cAMP-dependent protein kinase. S6 kinase elutes as a peak from DEAE-Sephacel at 100 mM NaC1, with an activity that is cAMP-dependent.
盘基网柄菌具有聚集能力的细胞提取物具有一种S6蛋白激酶活性，该活性在存在环磷酸腺苷（cAMP）依赖性蛋白激酶抑制剂的情况下会受到抑制。S6的磷酸化迅速，且迅速衰减。只有在存在于其他系统中用于保存S6激酶的磷酸酶抑制剂时，才能在150,000g上清液中检测到S6激酶活性，这表明该酶的活化形式是由cAMP依赖性蛋白激酶磷酸化的。S6激酶在100 mM NaCl条件下从DEAE-琼脂糖凝胶中以峰值形式洗脱，其活性依赖于cAMP。
