| Autor: |
Voznyi, Ya. V., Karpova, E. A., Dudukina, T. V., Tsvetkova, I. V., Boer, A. M., Janse, H. C., Diggelen, O. P. |
| Zdroj: |
Journal of Inherited Metabolic Disease; March 1993, Vol. 16 Issue: 2 p465-472, 8p |
| Abstrakt: |
Both the a- and ß-anomers of 4-methylumbelliferyl-D-glucosaminide were synthesized and shown to be substrates for the lysosomal acetyl-CoA: glucosaminideN-acetyltransferase. Using the ß-anomer, fibroblasts and leukocytes from 11 different Sanfilippo C patients showed <1% of mean normalN-acetyltransferase activity. Heterozygotes showed intermediate activities. The enzymatic liberation of the fluorochrome from 4-methylumbelliferyl-ß-d-glucosaminide requires the sequential action of theN-acetyltransferase and ß-hexosaminidase. Normal ß-hexosaminidase activity caused complete hydrolysis of the reaction intermediate 4-methylumbelliferyl-ß-d-N-acetylglucosaminide formed by theN-acetyltransferase. In cell extracts with a ß-hexosaminidase deficiency, however, a second incubation in the presence of excess ß-hexosaminidase is needed to avoid underestimation of theN-acetyltransferase activity. |
| Databáze: |
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