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Literature DB >> 5965332

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

R Virden, D C Watts, R L Watts, D B Gammack, J H Raper.

Abstract

1. The molecular weight of arginine kinase from lobster muscle has been determined by three procedures: ultracentrifuge analysis, gel filtration and density-gradient centrifugation. 2. The three methods give similar results and the best estimate of the molecular weight is 37000. 3. The enzyme does not readily show association-dissociation phenomena. 4. The usefulness of density-gradient centrifugation for determinations of molecular weight is briefly discussed.

Entities: Species

Mesh：

Substances：
Phosphotransferases

Year: 1966 PMID： 5965332 PMCID： PMC1264970 DOI： 10.1042/bj0990155

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

13 in total

1. [ACTIVE SITES OF ATP: ARGININE PHOSPHOTRANSFERASE].

Authors: L A PRADEL; R KASSAB; F REGNOUF
Journal: Biochim Biophys Acta Date: 1964-08-26

2. MOLECULAR EXCLUSION AND RESTRICTED DIFFUSION PROCESSES IN MOLECULAR-SIEVE CHROMATOGRAPHY.

Authors: G K ACKERS
Journal: Biochemistry Date: 1964-05 Impact factor: 3.162

3. APPARATUS FOR THE AUTOMATIC LOCATION OF ABSORBING COMPONENTS SEPARATED BY DENSITY GRADIENT CENTRIFUGATION.

Authors: J G EDWARDS; A P MATHIAS
Journal: Nature Date: 1963-08-10 Impact factor: 49.962

4. A method for determining the sedimentation behavior of enzymes: application to protein mixtures.

Authors: R G MARTIN; B N AMES
Journal: J Biol Chem Date: 1961-05 Impact factor: 5.157

5. High-Resolution Density Gradient Sedimentation Analysis.

Authors: R J Britten; R B Roberts
Journal: Science Date: 1960-01-01 Impact factor: 47.728

6. Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties.

Authors: L NODA; S A KUBY; H A LARDY
Journal: J Biol Chem Date: 1954-07 Impact factor: 5.157

7. Studies on adenosine triphosphate transphosphorylases. I. Amino acid composition of adenosine triphosphate-adenosine 5'-phosphate transphosphorylase (myokinase).

Authors: T A MAHOWALD; E A NOLTMANN; S A KUBY
Journal: J Biol Chem Date: 1962-04 Impact factor: 5.157

1. Evolutionary variation between a monomer and a dimer arginine kinase. Purification of the enzyme from Holothuria forskali and a comparison of some properties with that from Homarus vulgaris.

Authors: E O Anosike; B H Moreland; D C Watts
Journal: Biochem J Date: 1975-03 Impact factor: 3.857

2. Methods for starch-gel electrophoresis of sarcoplasmic proteins. An investigation of the relative mobilities of the glycolytic enzymes from the muscles of a variety of species.

Authors: R K Scopes
Journal: Biochem J Date: 1968-03 Impact factor: 3.857

6. Adenosine 5 -triphosphate--creatine phosphotransferase from dystrophic mouse skeletal muscle. A genetic lesion associated with the catalytic-site thiol group.

Authors: B T Hooton; D C Watts
Journal: Biochem J Date: 1966-09 Impact factor: 3.857

6 in total

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

1. [ACTIVE SITES OF ATP: ARGININE PHOSPHOTRANSFERASE].

2. MOLECULAR EXCLUSION AND RESTRICTED DIFFUSION PROCESSES IN MOLECULAR-SIEVE CHROMATOGRAPHY.

3. APPARATUS FOR THE AUTOMATIC LOCATION OF ABSORBING COMPONENTS SEPARATED BY DENSITY GRADIENT CENTRIFUGATION.

4. A method for determining the sedimentation behavior of enzymes: application to protein mixtures.

5. High-Resolution Density Gradient Sedimentation Analysis.

6. Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties.

7. Studies on adenosine triphosphate transphosphorylases. I. Amino acid composition of adenosine triphosphate-adenosine 5'-phosphate transphosphorylase (myokinase).

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

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

10. Estimation of the molecular weights of proteins by Sephadex gel-filtration.

1. Evolutionary variation between a monomer and a dimer arginine kinase. Purification of the enzyme from Holothuria forskali and a comparison of some properties with that from Homarus vulgaris.

2. Methods for starch-gel electrophoresis of sarcoplasmic proteins. An investigation of the relative mobilities of the glycolytic enzymes from the muscles of a variety of species.

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

4. Purification and properties of human serum cholinesterase.

5. The role of thiol groups in the structure and mechanism of action of arginine kinase.

6. Adenosine 5 -triphosphate--creatine phosphotransferase from dystrophic mouse skeletal muscle. A genetic lesion associated with the catalytic-site thiol group.