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BIOCHEMICAL STUDIES IN CAT AND HUMAN GANGLIOSIDOSIS 1, 2
Author(s) -
Handa S.,
Yamakawa T.
Publication year - 1971
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1971.tb00226.x
Subject(s) - gangliosidosis , tay sachs disease , ganglioside , ceramide , galactosidases , chemistry , hexosaminidase , glycoside hydrolase , enzyme , biochemistry , endocrinology , medicine , beta galactosidase , biology , disease , apoptosis , gene expression , gene
The biochemical analysis of the hereditary neurological disease found in a family of Siamese cat is reported. The accumulation of GM 1 ganglioside in the brain was noted. Several glycosidase activities of these cat brains were compared with that of human gangliosidoses (Tay‐Sachs disease and GM 1 ‐gangliosidosis). Glycosidase activities were estimated using ρ‐nitrophenyl‐glycosides, glucosyl‐, galactosyl‐ceramide and GM 1 ‐ganglioside as substrates. The results indicated the defect of the β‐galactosidase activities for the ρ‐nitrophenyl‐β‐galactoside and GM 1 ‐ganglioside in both cat and human GM 1 ‐gangliosidoses. Glycosidase activities for glucosyl‐ and galactosyl‐ceramide were not changed in either gangliosidoses.