Impaired degradation of chondroitin sulfate in GM2-gangliosidosis

Abstract
A new radiolabeled substrate was prepared, derived from chondroitin 6-sulfate oligosaccharide, for the assaying of chondroitin sulfate degradation by .beta.-N-acetylgalactosaminidase. Using this substrate, a striking deficiency of .beta.-N-acetylgalactosaminidase activity was found in the cultured skin fibroblasts of patients with Sandhoff disease and Tay-Sachs disease. DEAE-cellulose chromatography at pH 6.0 revealed that both isozymes A and B of .beta.-N-acetylgalactosaminidases from normal human liver participated in the catabolism of chondroitin 6-sulfate. There were major differences in substrate specificity between isoenzyme A and isoenzyme B.

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