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[Affinity modification of creatine kinase from rabbit skeletal muscles using gamma-(p-azidoanilide)-ATP].

Authors
  • Akopian, Zh I
  • Gazariants, M G
  • Mkrtchian, E S
  • Nersova, L S
  • Lavrik, O I
Type
Published Article
Journal
Biokhimii︠a︡ (Moscow, Russia)
Publication Date
Feb 01, 1981
Volume
46
Issue
2
Pages
262–268
Identifiers
PMID: 7018594
Source
Medline
License
Unknown

Abstract

Ultraviolet irradiation of creatine kinase (adenosine 5'-triphosphate: creatine-N-phosphotransferase, EC 2.7.3.2) in the presence of gamma-(p-azidoanilide)-[14C]-ATP results in a complete enzyme inactivation and covalent binding of two moles of analog per mole of enzyme. MgADP strongly protects the enzyme against inactivation. However, in the presence of MgADP the covalent binding of 0.9 moles of analog per mole of enzyme occurs without the enzyme inactivation. The rate of enzyme inactivation and covalent modification decreases in the presence of MgATP and creatine. These results indicate that gamma-(p-azidoanilide)-ATP is an affinity label for the active site of creatine kinase.

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