Comparative studies on creatine kinase isozymes from skeletal-muscle and stomach of trout
โ Scribed by Perriard, Jean-Claude ;Scholl, Adolf ;Eppenberger, Hans M.
- Publisher
- John Wiley and Sons
- Year
- 1972
- Tongue
- English
- Weight
- 535 KB
- Volume
- 182
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
โฆ Synopsis
Tissue-specific heterogeneity of creatine kinase (CPK) isozymes is particularly pronounced in various trout species. Several of the isozymes expressed in stomach and i n skeletal muscle appeared to be identical as judged by their electrophoretic behavior, but reversible dissociation studies on single, electrophoretically pure, CPK-isozymes isolated from these two tissues revealed significant differences between isozymes of similar electrophoretic mobility. Moreover, in contrast to trout skeletal muscle, the native and reassociated stomach CPK isozyme patterns could be accounted for by the association of the polypeptide products of two gene loci into homodimers and heterodimers, providing further evidence that the isozymes of stomach and skeletal muscle are non-identical and thus presumably the products of distinct genes.
๐ SIMILAR VOLUMES
The steady-state kinetics of the creatine kinase reaction in rabbit skeletal muscle in vivo was investigated using inversion and saturation magnetization transfer techniques. Both techniques determined the forward rate of this reaction (creatine phosphate ATP) as approximately 0.3 s-1. This correspo
The urinary bladder depends on intracellular ATP for the support of a number of essential intracellular processes including contraction. The concentration of ATP is maintained constant primarily via the rapid transfer of a phosphate from creatine phosphate (CP) to ADP catalyzed by the enzyme creatin