G(M2) GANGLIOSIDE ACTIVATOR OCCURS IN MULTIPLE FORMS

The protein which activates the hydrolysis of G(M2) ganglioside by hex osaminidase A was purified from human kidney. The G(M2) activator had a molecular mass of 28 kDa by gel filtration and was resolved into thr ee major bands using polyacrylamide gel electrophoresis in the presenc e of SDS with molecular masses of 23, 22 and 21 kDa. These three bands corresponded respectively to strongly binding, weakly binding and non -binding fractions of G(M2) activator chromatographed through concanav ilin A-Sepharose, indicating that G(M2) activator exists in multiple g lycosylated forms.