• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of biochemjBJ Latest papers and much more!
Biochem J. Mar 1965; 94(3): 536–544.
PMCID: PMC1206586

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.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.2M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • BEAVEN GH, HOLIDAY ER. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. [PubMed]
  • COHN M. MAGNETIC RESONANCE STUDIES OF METAL ACTIVATION OF ENZYMIC REACTIONS OF NUCLEOTIDES AND OTHER PHOSPHATE SUBSTRATES. Biochemistry. 1963 Jul-Aug;2:623–629. [PubMed]
  • FLORINI JR, VESTLING CS. Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta. 1957 Sep;25(3):575–578. [PubMed]
  • GAMMACK DB, HUEHNS ER, SHOOTER EM, GERALD PS. Identification of the abnormal polypeptide chain of hemoglobin G-Ib. J Mol Biol. 1960 Dec;2:372–378. [PubMed]
  • Goodwin TW, Morton RA. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J. 1946;40(5-6):628–632. [PMC free article] [PubMed]
  • Green DE, Needham DM, Dewan JG. Dismutations and oxidoreductions. Biochem J. 1937 Dec;31(12):2327–2352. [PMC free article] [PubMed]
  • KUBY SA, NODA L, LARDY HA. Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J Biol Chem. 1954 Jul;209(1):191–201. [PubMed]
  • MORRISON JF, GRIFFITHS DE, ENNOR AH. The purification and properties of arginine phosphokinase. Biochem J. 1957 Jan;65(1):143–153. [PMC free article] [PubMed]
  • NODA L, KUBY SA, LARDY HA. Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties. J Biol Chem. 1954 Jul;209(1):203–210. [PubMed]
  • NODA L, NIHEI T, MORALES MF. The enzymatic activity and inhibition of adenosine 5'-triphosphate-creatine transphosphorylase. J Biol Chem. 1960 Oct;235:2830–2834. [PubMed]
  • NOLTMANN EA, MAHOWALD TA, KUBY SA. Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase. J Biol Chem. 1962 Apr;237:1146–1154. [PubMed]
  • O'SULLIVAN WJ, PERRIN DD. The stability constants of MgATP -2 ion. Biochim Biophys Acta. 1961 Sep 30;52:612–614. [PubMed]
  • SZORENYI E, ELODI P, DEVENYI T. Uber einige enzymatische und chemische Eigenschaften der aus Krebsarten kristallin isolierten D-Glycerinaldehyd-3-Phosphat Dehydrogenase. Acta Physiol Hung. 1956;9(4):351–365. [PubMed]
  • VIRDEN R, WATTS DC. THE DISTRIBUTION OF GUANIDINE-ADENOSINE TRIPHOSPHATE PHOSPHOTRANSFERASES AND ADENOSINE TRIPHOSPHATASE IN ANIMALS FROM SEVERAL PHYLA. Comp Biochem Physiol. 1964 Oct;13:161–177. [PubMed]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...