Studies on Adenosine Triphosphate Transphosphorylases

The isolation of the crystalline enzymes, adenosine triphosphate-creatine transphosphorylase (1) and adenosine triphosphate-adenosine 5’-phosphate transphosphorylase (2), made possible a comparative approach to the general problem of the mechanism of action of the adenosine triphosphate transphosphorylases. The present series of papers extends earlier studies from this laboratory on these enzymes (3-6) and was undertaken specifically to compare the molecular properties of both proteins. A quantitative amino acid analysis is the basis for any sequence studies and provides the foundation for a chemical evaluation of the enzymic reaction and the relationship between the chemical and physical properties of the protein. Paper I is concerned with the amino acid composition of the adenosine triphosphate-adenosine 5’-phosphate transphosphorylase (myokinase) ; preliminary results of this work have been presented (7).