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β ‐D‐galactosidase activities in juvenile GM 1 ‐gangliosidosis
Author(s) -
Hultberg Bjourn,
Sjoublad Sture
Publication year - 1978
Publication title -
acta neurologica scandinavica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.967
H-Index - 95
eISSN - 1600-0404
pISSN - 0001-6314
DOI - 10.1111/j.1600-0404.1978.tb02882.x
Subject(s) - galactosidases , galactoside , beta galactosidase , substrate (aquarium) , chemistry , ceramide , oligosaccharide , beta (programming language) , biochemistry , enzyme , stereochemistry , biology , ecology , apoptosis , gene expression , computer science , programming language , gene
β‐Galactosidase activity was investigated in one case of juvenile GM 1 ‐gangliosidosis. This patient exhibited normal activity of the neutral form of β‐galactosidase (measured as β‐glucosidase activity) and normal pH curve of residual acid β‐galactosidase activity in leucocytes and fibroblasts. A shift towards more neutral pH optimum was seen in the β‐galactosidase enzyme occurring in serum. The communication also presents a study of the relationship of the different β‐galactosidases in human liver using isolated urine oligosaccharide from this patient as a β‐galactoside substrate. The other natural β‐galactoside substrates used in this investigation were different oligosaccharides, one glycopeptide and ceramide‐β‐galactoside. The β‐galactosidase forms with acidic pH optimum towards synthetic substrate (A forms) exhibit activity towards the natural substrate (except ceramide‐β‐galactoside). The “neutral”β‐galactosidase with broad substrate specificity (B form) which includes β‐glucosides had no activity towards the natural substrates used. It could also be shown that the activity towards ceramide‐β‐galactoside was a third type of β‐galactosidase different from A and B forms.