K,-cells from Drosophila melanogaster, grown under serum-free conditions, produce two p-hexosaminidases and secrete these enzymes into the medium. The two enzymes were separated by DEAE-exchange chromatography. According to their substrate specificities one enzyme is a f3-N-acetyl-D-glucosarninidase
Analysis of n-acetyl-β-d-glucosaminidase in mucolipidosis II (I-cell disease)
✍ Scribed by Kari Kveim Lie; George H. Thomas; Harold A. Taylor; Judith A. Sensenbrenner
- Book ID
- 115820102
- Publisher
- Elsevier Science
- Year
- 1973
- Tongue
- English
- Weight
- 425 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0009-8981
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Serum N-acetyl-beta-D-hexosaminidase is compared quantitatively and qualitatively in 14 obligate heterozygotes for the mutant gene causing I cell disease (ICD) or mucolipidosis II and in 31 normal controls. The average specific activity in either group is significantly different but reliable heteroz
Kc-cells from Drosophila produce two different beta-D-hexosaminidases, a beta-N-acetyl-D-glucosaminidase (E.C.3.2.1.30) and a beta-N-acetyl-D-hexosaminidase (E.C.3.2.1.52), which are also secreted into the medium. The Mr of both enzymes is about 126,000 +/- 9,700; the S-values are 8.37 +/- 0.44. Bot
Isozymes of N-acetyl-beta-D-hexosaminidase in body fluids, culture medium, postmortem organs, and cultured fibroblasts from patients with I-cell disease were resolved by ion exchange column chromatography. The elution pattern was compared in detail with that of the isozymes in control samples. This