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Chemically the reac­ tions catalyzed by viral reverse transcriptases are identical. One cannot distinguish an avian from a primate enzyme. A l s o , the polymerase of a "foamy" virus (not proven to be oncogenic) cannot be distin­ guished by the chemical reactions it catalyzes from the polymerase of a primate C-type oncogenic virus. In addition, since C-type viruses of many species can 59 EDWARD M. SCOLNICK grow in human cells and since, especially in cell cul­ ture, inadvertant infection does occur, it is impor­ tant to be able to identify the species of origin of a virus with a reverse transcriptase.

J[. Neuropath. Exp . Neurol. 2 2 , 1 8 , 1963. , Patabiraman, T. , and Bachhawat, B,, A controlled study of enzymic activities in three human disorders of glycolipid metabolism. ,J. , 10, 805 (1963). , Com­ position and synthesis of gangliosides in rat hepatocyte and hepatoma cell lines. J[. Biol. , 244, 6552 (1969). , Gal, A . E . , Enzyma­ tic defect in Fabry's disease: ceramide trihexosidase deficiency. New Eng. J_. , 276, 1163 (1967). , Identification of heterozygous carriers of lipid storage diseases.

28) (9) . 0 2 4 6 8 10 DISTANCE Fig. 28. 12 14 16 18 (cm) Labelling of gangliosides in tissue culture. We therefore began direct investigation of gan­ glioside catabolism. The catabolism of the most prev­ alent gangliosides, &£>± and ^ 3 , is initiated by the cleavage of the molecule of N-acetylneuraminic acid linked to the terminal molecule of galactose (Fig. 2 9 ) . These gangliosides were biosynthetically labeled in the sialic acid port ion of the molecule (17)· Tests with these labeled materials as substrates indicated that ganglioside catabolism was not accelerated in the virally transformed cells ( 1 2 ) .

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