Properties of a CH3-blocked creatine kinase with altered catalytic activity. Kinetic consequences of the presence of the blocking group.
Open Access
- 1 February 1977
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (4) , 1202-1207
- https://doi.org/10.1016/s0021-9258(17)40641-7
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymesBiochemistry, 1975
- Prediction of protein conformationBiochemistry, 1974
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- The interaction of nucleotides with kinases, monitored by changes in protein fluorescenceFEBS Letters, 1972
- Protein foldingJournal of the American Chemical Society, 1972
- Barriers to rotation about the sulfur-sulfur bond in acyclic disulfidesJournal of the American Chemical Society, 1971
- Isotope Exchange Studies of the Reaction Catalyzed by ATP: Creatine PhosphotransferaseEuropean Journal of Biochemistry, 1967
- Regulation of Enzyme ActivityAnnual Review of Biochemistry, 1966
- Amino-Acid Sequence Around the Reactive Thiol Groups of Adenosine Triphosphate–creatine PhosphotransferaseNature, 1964
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963