Isolation and characterization of sea urchin flagellar creatine kinase

Phosphagen kinases play a role in metabolic function in diverse species (Bessman and Carpenter, 1985). Enzyme assays and inhibitors have been used successfully to demonstrate the role of one of these enzyme families in sea urchins. Although arginine kinase was not purified, its enzymatic activity has been detected in sea urchin eggs and embryos and many other species by simply substituting phosphoarginine (PArg) for PCr (Fujimaki and Yanagisawa, 1978; Tombes and Shapiro, 1989). ArgK does not show sensitivity to FDNB, but CrK proteins of the appropriate molecular weight were detected with this reagent in cells from many species (Tombes and Shapiro, 1989). The use of these techniques to identify and study function of phosphagen kinases in diverse species has much potential.