Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3',5'-AMP-stimulated protein kinase. |
| |
Authors: | Elisabet Humble Lars Berglund Vincent Titanji Olle Ljungström Bror Edlund Örjan Zetterqvist Lorentz Engström |
| |
Institution: | Institute of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala, S-751 23 Uppsala, Sweden |
| |
Abstract: | Alkali-inactivated pig liver pyruvate kinase, type L, and a cyanogen bromide fragment from the same enzyme were shown to be phosphorylated by (32P)ATP and cyclic 3′,5′-AMP-stimulated protein kinase. In both cases the rate of phosphorylation was higher than with the native enzyme. Pyruvate kinases types A and M were not phosphorylated under the same conditions. From the 32P-labelled cyanogen bromide fragment (32P)phosphorylserine was isolated. The electrophoretic pattern of (32P)phosphopeptides obtained on partial acid hydrolysis of the fragment indicated that the phosphorylated site of the fragment was identical with that of the native pyruvate kinase. |
| |
Keywords: | cAMP cyclic 3′5′-adenosine monophosphate |
本文献已被 ScienceDirect 等数据库收录! |