BACTERIAL ASPARTATE KINASE-LIKE ACTIVITY IN HUMAN PLATELET

One form of a group of enzymes known as aspartate kinases, primarily r eported in prokaryotes and plants, might also exist in animal cells. W ere we report the immunodetection of an aspartate kinase-like activity in human platelets using antibodies against the pure form of the enzy me purified from Escherichia coli. Moreover, the enrichment of platele t extracts with the bacterial kinase results in the phosphorylation of discrete forms mainly of membrane-bound endogenous polypeptides.