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. 1965 Mar;94(3):536–544. doi: 10.1042/bj0940536

Adenosine 5′-triphosphate–arginine phosphotransferase from lobster muscle: purification and properties

R Virden 1, D C Watts 1, E Baldwin 1
PMCID: PMC1206586  PMID: 14340045

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BEAVEN G. H., HOLIDAY E. R. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. doi: 10.1016/s0065-3233(08)60022-4. [DOI] [PubMed] [Google Scholar]
  2. COHN M. MAGNETIC RESONANCE STUDIES OF METAL ACTIVATION OF ENZYMIC REACTIONS OF NUCLEOTIDES AND OTHER PHOSPHATE SUBSTRATES. Biochemistry. 1963 Jul-Aug;2:623–629. doi: 10.1021/bi00904a001. [DOI] [PubMed] [Google Scholar]
  3. FLORINI J. R., VESTLING C. S. Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta. 1957 Sep;25(3):575–578. doi: 10.1016/0006-3002(57)90529-2. [DOI] [PubMed] [Google Scholar]
  4. GAMMACK D. B., HUEHNS E. R., SHOOTER E. M., GERALD P. S. Identification of the abnormal polypeptide chain of hemoglobin G-Ib. J Mol Biol. 1960 Dec;2:372–378. doi: 10.1016/s0022-2836(60)80048-4. [DOI] [PubMed] [Google Scholar]
  5. Goodwin T. W., Morton R. A. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J. 1946;40(5-6):628–632. doi: 10.1042/bj0400628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Green D. E., Needham D. M., Dewan J. G. Dismutations and oxidoreductions. Biochem J. 1937 Dec;31(12):2327–2352. doi: 10.1042/bj0312327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KUBY S. A., NODA L., LARDY H. A. Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J Biol Chem. 1954 Jul;209(1):191–201. [PubMed] [Google Scholar]
  8. MORRISON J. F., GRIFFITHS D. E., ENNOR A. H. The purification and properties of arginine phosphokinase. Biochem J. 1957 Jan;65(1):143–153. doi: 10.1042/bj0650143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. NODA L., KUBY S. A., LARDY H. A. Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties. J Biol Chem. 1954 Jul;209(1):203–210. [PubMed] [Google Scholar]
  10. NODA L., NIHEI T., MORALES M. F. The enzymatic activity and inhibition of adenosine 5'-triphosphate-creatine transphosphorylase. J Biol Chem. 1960 Oct;235:2830–2834. [PubMed] [Google Scholar]
  11. NOLTMANN E. A., MAHOWALD T. A., KUBY S. A. Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase. J Biol Chem. 1962 Apr;237:1146–1154. [PubMed] [Google Scholar]
  12. O'SULLIVAN W. J., PERRIN D. D. The stability constants of MgATP -2 ion. Biochim Biophys Acta. 1961 Sep 30;52:612–614. doi: 10.1016/0006-3002(61)90431-0. [DOI] [PubMed] [Google Scholar]
  13. SZORENYI E., ELODI P., DEVENYI T. Uber einige enzymatische und chemische Eigenschaften der aus Krebsarten kristallin isolierten D-Glycerinaldehyd-3-Phosphat Dehydrogenase. Acta Physiol Acad Sci Hung. 1956;9(4):351–365. [PubMed] [Google Scholar]
  14. VIRDEN R., WATTS D. C. THE DISTRIBUTION OF GUANIDINE-ADENOSINE TRIPHOSPHATE PHOSPHOTRANSFERASES AND ADENOSINE TRIPHOSPHATASE IN ANIMALS FROM SEVERAL PHYLA. Comp Biochem Physiol. 1964 Oct;13:161–177. doi: 10.1016/0010-406x(64)90202-6. [DOI] [PubMed] [Google Scholar]

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