Molecular Weight Isoenzymes of Arginine Kinase in the Mollusca and their Association with Muscle Function
- 1 September 1967
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 215 (5105), 1092-1094
- https://doi.org/10.1038/2151092a0
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Phosphagen Kinases and Evolution in the EchinodermataNature, 1967
- Hétéroenzymes d'acide adénosine 5′-triphosphorique: L-arginine phosphotransféraseBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weightBiochemical Journal, 1966
- Creatine kinase: Evidence for a dimeric structureBiochemical and Biophysical Research Communications, 1965
- The distribution of guanidine-adenosine triphosphate phosphotransferases and adenosine triphosphatase in animals from several phylaComparative Biochemistry and Physiology, 1964
- Sites actifs de l'atp:arginine phosphotransféraseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- The ontogeny of creatine kinase isozymesDevelopmental Biology, 1964
- Second Acid Dissociation of N,N-Di(2-hydroxyethyl)glycine and Related Thermodynamic Quantities from 0 to 55°The Journal of Physical Chemistry, 1964
- Coupled Reaction of Creatine Kinase and Myosin A-Adenosine TriphosphataseJournal of Biological Chemistry, 1962