| Literature DB >> 14340045 |
R VIRDEN, D C WATTS, E BALDWIN.
Abstract
1. A simple chromatographic method is described for the purification of arginine kinase from lobster (Homarus vulgaris) muscle. 2. Some physical properties and the effects on enzyme activity of ionic strength, pH, buffer salts, metal ions and substrates are reported. 3. The kinetic parameters, evaluated by variation of the concentration of one of the substrates, are dependent on the concentration of the other substrate. 4. The properties of the enzyme are discussed in relation to previous findings about phosphagen phosphotransferases.Entities:
Keywords: ADENOSINE TRIPHOSPHATE; ARGININE; BIOCHEMISTRY; CHROMATOGRAPHY; CRUSTACEA; ELECTROPHORESIS; EXPERIMENTAL LAB STUDY; GEL FILTRATION; MUSCLES; PHOSPHOTRANSFERASES; ULTRACENTRIFUGATION
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Year: 1965 PMID: 14340045 PMCID: PMC1206586 DOI: 10.1042/bj0940536
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857