Properties and reaction with iodoacetamide of adenosine 5′-triphosphate–creatinine phosphotransferase from human skeletal muscle. Further evidence about the role of the essential thiol group in relation to the mechanism of action

Ítems similars

• Further evidence for the role of the essential thiol groups in adenosine triphosphate-creatine phosphotransferase from a comparison of the human and rabbit enzymes.
  per: Watts, D C, et al.
  Publicat: (1970)
• The significance of anions in the protection by substrates of adenosine triphosphate-creatine phosphotransferase against inhibition by iodoacetamide.
  per: Milner-White, E J, et al.
  Publicat: (1970)
• Formation of an unusual hybrid in the development of human adenosine 5′-triphosphate–creatine phosphotransferase
  per: Kumudavalli, I., et al.
  Publicat: (1968)
• Adenosine 5′-triphosphate–creatine phosphotransferase from dystrophic mouse skeletal muscle. A genetic lesion associated with the catalytic-site thiol group
  per: Hooton, B. T., et al.
  Publicat: (1966)
• The conversion of adenosine 5′-phosphate into adenosine triphosphate as catalysed by adenosine triphosphate–creatine phosphotransferase and adenosine triphosphate–adenosine monophosphate phosphotransferase in the presence of phosphocreatine
  per: Doherty, M. D., et al.
  Publicat: (1963)