Temperature dependence of arginine kinase reaction in the tail muscle of live Sycionia ingentis as measured in vivo by 31P-NMR driven saturation transfer

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11 Scopus citations

Abstract

We have employed the driven 31P-NMR saturation transfer method to measure in vivo the temperature dependence of the forward and reverse unidirectional fluxes of the arginine kinase reaction in the tail muscle of a live shrimp, Sycionia ingentis. Our results indicated that neither the forward nor the reverse rate constants of this reaction were significantly temperature-dependent between 8 and 16°C, in contrast to the kinetic characteristics of isolated arginine kinases.

Original languageEnglish
Pages (from-to)44-49
Number of pages6
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1135
Issue number1
DOIs
StatePublished - Apr 30 1992

Bibliographical note

Funding Information:
The authors are grateful for the financial support (rum the U.S. Departmenotf Interior grant No. 14-35-flll~ll-3f1471W. e wish to also thank Dr. W.H. Clark and his team. ~.~,peciallyD r. Fred Griffin. Athula Wikra-manayakca, nd Philfip Hertzler for their generousg ift of the shrimp. Finally. we are in debt to Dr. Gary Cherr for his valuables uggestions.

Keywords

  • (Sycionia ingentis)
  • Arginine kinase
  • NMR, P-
  • Tail muscle

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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