Abstract
4-Methylumbelliferyl α-ketoside of N-acetylneuraminic acid was synthesized by reacting the sodium salt of 4-methylumbelliferone with the 2-chloro-2-deoxy derivative of peracetylated methyl N-acetylneuraminate, followed by preparative silica gel chromatography, deblocking, and purification by gel filtration on Sephadex G-25. The final product was isolated as either the sodium or ammonium salt, and its suitability as a substrate for neuraminidase was evaluated. The optimal pH values for various neuraminidases were 5.6 in acetate buffer (Arthrobacter ureafaciens), 5.0-5.1 in acetate buffer (Clostridium perfringens), and 4.4 in phosphate-citrate buffer (human fibroblasts). Km values for these enzymes at the optimal pH were 6 × 10-4 m (Arthrobacter), 1 × 10-4 m (Clostridium), and 3 × 10-4 m (human fibroblasts).
Original language | English (US) |
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Pages (from-to) | 166-174 |
Number of pages | 9 |
Journal | Analytical biochemistry |
Volume | 101 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 1980 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology