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. 1983;2(7):1201–1205. doi: 10.1002/j.1460-2075.1983.tb01567.x

Variant of GM2-gangliosidosis with hexosaminidase A having a severely changed substrate specificity.

H J Kytzia, U Hinrichs, I Maire, K Suzuki, K Sandhoff
PMCID: PMC555256  PMID: 6226523

Abstract

The levels of hexosaminidase A activity in cultivated fibroblasts of two patients with GM2-gangliosidosis were close to the normal range with 4-methylumbelliferyl-beta-D-2-acetamido-2-deoxyglucopyranoside and 4-methylumbelliferyl-beta-D-2-acetamido-2-deoxygalactopyranoside as substrates, and the enzymes were normal in most parameters analyzed. However, the enzymes of both patients were almost completely inactive against two specific substrates for hexosaminidase A, rho-nitrophenyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside, and ganglioside GM2 in the presence of GM2-activator. Fibroblast extracts of both patients showed normal hexosaminidase B and GM2-activator activity, the latter was strongly decreased in two cases with variant AB. It is suggested that human hexosaminidase A may contain two different active sites which might be inactivated separately by different mutations.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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