Walter R D
Hoppe Seylers Z Physiol Chem. 1978 May;359(5):601-6. doi: 10.1515/bchm.1978.359.1.601.
Three protein kinases were distinguished in Trypanosoma gambiense extract. The enzymes preferred phosvitin, histone, and protamine as acceptor proteins, respectively. The amino acid residues of the acceptor proteins which were phosphorylated by these protein-kinase activities were serine and- to less extent- threonine. The protein kinase activities were neither affected by cyclic nucleotides nor by cyclic AMP receptors. The molecular weights of these protein kinases were determined to be greater than 200,000, 95000 and 37000, respectively. The activities of all three protein kinases were affected to varying degrees by nucleotides and nucleosides.
在冈比亚锥虫提取物中鉴别出了三种蛋白激酶。这些酶分别偏好磷蛋白、组蛋白和鱼精蛋白作为受体蛋白。被这些蛋白激酶活性磷酸化的受体蛋白的氨基酸残基是丝氨酸，苏氨酸的磷酸化程度较低。这些蛋白激酶活性既不受环核苷酸影响，也不受环磷酸腺苷受体影响。这些蛋白激酶的分子量分别测定为大于200,000、95,000和37,000。所有三种蛋白激酶的活性都受到核苷酸和核苷不同程度的影响。
