A simplified and rapid method for simultaneous activity measurements of three lysosomal marker enzymes, acid phosphatase, beta-glucuronidase, and beta-N-acetyl-D-hexosaminidase is described. The incubation is carried out in a single test tube and stopped by adding an alkaline sodium dodecyl sulfate
Synthesis of disaccharide derivatives employing β-N-acetyl- d-hexosaminidase, β-d-galactosidase and β-d-glucuronidase
✍ Scribed by Kurt G.I. Nilsson; Anna Eliasson; Hefeng Pan; Mattias Rohman
- Book ID
- 110224784
- Publisher
- Springer Netherlands
- Year
- 1999
- Tongue
- English
- Weight
- 64 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0141-5492
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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
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