Multiple Protein Kinases from Trypanosoma gambiense
- 1 January 1978
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry
- Vol. 359 (1) , 601-606
- https://doi.org/10.1515/bchm.1978.359.1.601
Abstract
Protein kinases (3) were distinguished in T. 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 lesser extent, threonine. The protein kinase activities were neither affected by cyclic nucleotides nor by cyclic AMP receptors. The MW of these protein kinases were > 200,000, 95,000 and 37,000, respectively. The activities of all 3 protein kinases were affected to varying degrees by nucleotides and nucleosides.This publication has 2 references indexed in Scilit:
- Adenosine 3′,5′-Cyclic Monophosphate-Binding Proteins from Trypanosoma gambienseBiological Chemistry, 1978
- Inhibitory effects of cordycepin on cyclic nucleotide-dependent and cyclic nucleotide-independent protein kinasesBiochemical Pharmacology, 1977