Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weight
- 1 April 1966
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 99 (1), 155-158
- https://doi.org/10.1042/bj0990155
Abstract
The molecular weight of arginine kinase from lobster muscle has been determined by 3 procedures ultracentrifuge analysis, gel filtration and density-gradient centrifugation. The three methods give similar results and the best estimate of the molecular weight is 37,000. The enzyme does not readily show association[long dash]dissociation phenomena. The usefulness of density gradient centrifugation for determinations of molecular weight is briefly discussed.This publication has 16 references indexed in Scilit:
- Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle. Amino acid compositionBiochemical Journal, 1966
- The distribution of guanidine-adenosine triphosphate phosphotransferases and adenosine triphosphatase in animals from several phylaComparative Biochemistry and Physiology, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- Molecular Exclusion and Restricted Diffusion Processes in Molecular-Sieve Chromatography*Biochemistry, 1964
- Apparatus for the Automatic Location of Absorbing Components separated by Density Gradient CentrifugationNature, 1963
- STUDIES ON ADENOSINE TRIPHOSPHATE TRANSPHOSPHORYLASES .1. AMINO ACID COMPOSITION OF ADENOSINE TRIPHOSPHATE-ADENOSINE 5'-PHOSPHATE TRANSPHOSPHORYLASE (MYOKINASE)1962
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961
- High-Resolution Density Gradient Sedimentation AnalysisScience, 1960
- Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle.1956
- ADENOSINETRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE .2. HOMOGENEITY AND PHYSICOCHEMICAL PROPERTIES1954