Further evidence for the role of the essential thiol groups in adenosine triphosphate-creatine phosphotransferase from a comparison of the human and rabbit enzymes.

Míreanna Comhchosúla

• 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
  le: Kumudavalli, I., et al.
  Foilsithe: (1970)
• Formation of an unusual hybrid in the development of human adenosine 5′-triphosphate–creatine phosphotransferase
  le: Kumudavalli, I., et al.
  Foilsithe: (1968)
• Brain adenosine 5′-triphosphate–creatine phosphotransferase. Purification, thiol group reactivity and the amino acid sequence around the reactive thiol groups
  le: Atherton, R. S., et al.
  Foilsithe: (1970)
• A study of the `reactive' sulphydryl groups of adenosine 5′-triphosphate–creatine phosphotransferase
  le: Watts, D. C., et al.
  Foilsithe: (1962)
• Adenosine 5′-triphosphate–creatine phosphotransferase from dystrophic mouse skeletal muscle. A genetic lesion associated with the catalytic-site thiol group
  le: Hooton, B. T., et al.
  Foilsithe: (1966)