Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase
- 13 October 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (21) , 6155-6164
- https://doi.org/10.1021/bi00524a038
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Preparation and properties of chromium(III) adenosine 5'-triphosphate, chromium(III) adenosine 5'-diphosphate, and related chromium(III) complexesBiochemistry, 1980
- Creatine kinase. Nuclear magnetic resonance and fluorescence evidence for interaction of adenosine 5'-diphosphate with aromatic residue(s)Biochemistry, 1979
- The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonateBiochemical Journal, 1979
- Affinity labeling of creatine kinase by N-(2,3-epoxypropyl)-N-amidinoglycine.Journal of Biological Chemistry, 1979
- Studies on Adenosine Triphosphate Transphosphorylases. V. Studies on the Polypeptide Chains of the Crystalline Adenosine Triphosphate-Creatine Transphosphorylase from Rabbit Skeletal Muscle*Biochemistry, 1967
- Isotope Exchange Studies of the Mechanism of the Reaction Catalyzed by Adenosine Triphosphate: Creatine PhosphotransferaseJournal of Biological Chemistry, 1966
- The mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferaseBiochemical Journal, 1965
- Creatine and Creatine Kinase MeasurementJournal of Biological Chemistry, 1959
- ADENOSINETRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE .1. ISOLATION OF THE CRYSTALLINE ENZYME FROM RABBIT MUSCLE1954
- ADENOSINETRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE .2. HOMOGENEITY AND PHYSICOCHEMICAL PROPERTIES1954