o-phthalaldehyde for the fluorometric assay of nonprotein amino compounds. |
| |
Authors: | D J Reeder L T Sniegoski R Schaffer |
| |
Institution: | Department of Biochemistry, University of Georgia, Athens, Georgia 30602 USA |
| |
Abstract: | Procedures for the preparation of UDP-N-1-14C]acetyl-d-glucosamine and UDP-N-1-14C]acetyl-d-galactosamine with very high specific activities are deseribed. The overall yield based on the amount of 1-14C]acetate used is greater than 80%. The N-acetyl-d-glucosamine-α-1-phosphate used in this synthesis is prepared by phosphorylation of tetraacetyl-d-N-acetylglucosamine with crystalline phosphoric acid. N-acetyl-d-glucosamine-α-1-phosphate is then deacetylated in anhydrous hydrazine with hydrazine sulfate as a catalyst. d-glucosamine-α-1-phosphate is N-acetylated with 14C]acetate using N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline as the coupling agent. The acetylated product is coverted to the UDP derivative with yeast UDP-N-acetyl-d-glucosamine pyrophosphorylase. UDP-N-1-14C]acetylgalactosamine is prepared by acetylation of UDP-galactosamine using 1-14C]acetate and N-ethoxy-carbonyl-2-ethoxy-1,2-dihydroquinoline. UDP-galactosamine is prepared enzymatically using galactokinase and galactose-1-phosphate uridyltransferase. The labeled products, isolated and characterized by ion-exchange and paper chromatography, were active as substrates in glycosyl transferase systems. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|