Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.4.99.6 (sialyltransferase)
 1,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

CDP-hexanolamine agarose was used as an affinity adsorbent to purify a CMP-N-acetylneuraminate: beta-D-galactosyl-glycoprotein N-acetylneuraminyltransferase (EC 2.4.99.1) from bovine colostrum. Upon binding of the enzyme to the adsorbent, elution is achieved either nonspecifically, with 0.5 to 1.0 M sodium chloride, or specifically, with CDP. A highly purified sialyltransferase is obtained with a specific activity 440,000 times that of whole colostrum. Fractionation of the purified enzyme by gel filtration gives two species with different molecular weights but equal specific activities toward asialo-alpha1-acid glycoprotein (26.0 to 28.0 micronmol/min/mg of enzyme). The molecular weights of these two forms are about 56,000 and 43,000 as judged by sodium doedcyl sulfate-gel electrophoresis, sedimentation equilibrium, and gel filtration. The catalytic properties of both forms have been examined (Paulson, J. C., Rearick, J. I., and Hill, R. L. (1977) J. Biol. Chem. 252, 2363-2371). It is concluded that the lower molecular weight form may be a partially degraded species of the enzyme of higher molecular weight.
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PMID:Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. 84 32

An assay method for glycosphingolipid glycosyltransferase activity using simple Sephadex G-50 gel permeation chromatography in an aqueous solvent has been developed. An acceptor glycosphingolipid and a donor radioactive nucleotide sugar were incubated with an enzyme source. The reaction mixture was loaded onto a Sephadex G-50 column previously equilibrated with 0.3% (w/v) Triton X-100, 0.1 M sodium chloride, and 0.02% (w/v) sodium azide. The radiolabeled reaction product was eluted by the same solvent in the excluded volume and was collected directly into a liquid scintillation vial, separated from other radioactive compounds. This assay method was utilized to determine the activity of cytidine 5'-monophosphate-N-acetylneuraminic acid:GM3 ganglioside sialyltransferase, which catalyzes the synthesis of GD3 ganglioside, and proved to be as reliable and sensitive as previously published assay procedures. In addition, this assay can be carried out in less time and is simpler than previously reported procedures.
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PMID:Glycosphingolipid glycosyltransferase assay using sephadex G-50 chromatography in aqueous phase. 367 12