Identity of the activator proteins for the enzymatic hydrolysis of sulfatide, ganglioside GM1, and globotriaosylceramide.

The activator protein for the enzymatic hydrolysis of sulfatide, ganglioside GM1, and globotriaosylceramide was purified from human kidney, brain, and urine. As far as they could be assayed, these three activities cochromatographed during all steps, indicating that they are due to the same protein. This result was corroborated by immunochemical comparison of individually purified activator preparations. In contrast, the activator for ganglioside GM2 hydrolysis could clearly be separated from the other activities. Kinetic data were determined for the interaction of the sulfatide activator with the different glycolipids and hydrolases.