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ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES.

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.

SUBMITTER: VIRDEN R

PROVIDER: S-EPMC1206586 | biostudies-other | 1965 Mar

REPOSITORIES: biostudies-other

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Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle.

Project description:1. The amino acid composition of lobster-muscle arginine kinase is given and discussed briefly. 2. The results were used to calculate a partial specific volume of 0.735. 3. The results are compared with the amino acid composition of creatine kinase.

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Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weight.

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Brain adenosine 5'-triphosphate-creatine phosphotransferase.

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Multiple forms of glucose-adenosine triphosphate phosphotransferase in rat mammary gland.

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Further properties and possibel mechanism of action of adenosine 5'-triphosphate-D-glucose 6-phosphotransferase from rat liver.

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Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue.

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