G M2 ganglioside activator occurs in multiple forms

Abstract

The protein which activates the hydrolysis of G M2 ganglioside by hexosaminidase A was purified from human kidney. The G M2 activator had a molecular mass of 28 kDa by gel filtration and was resolved into three major bands using polyacrylamide gel electrophoresis in the presence 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 concanavilin A-Sepharose, indicating that G M2 activator exists in multiple glycosylated forms.