By Alton Meister
Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative stories of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the historic improvement of enzymology. The sequence bargains researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic technique, and their program in either the laboratory and undefined. each one quantity within the sequence beneficial properties contributions via best pioneers and investigators within the box from all over the world. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety of subject matters and lengthy historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally through any scientist attracted to the invention of an enzyme, its homes, and its applications.
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
As estimated by gel electrophoresis and by sedimentation equilibrium methods, which were in close agreement, the molecular weights of sialyltransferase I and I1 were approximately 56,000 and 43,000, respectively. By analytical gel filtration chromatography using globular protein standards, sialyltransferase I1 was estimated to have a molecular weight of 45,000, in good agreement with that determined by electrophoresis and centrifugation. However, under the same chromatographic conditions sialyltransferase I behaved as a globular protein with a molecular weight of 80,000.
2. 0-Galactoside a2+6 Sialy ltransferase The first sialyltransferase to be purified to homogeneity was isolated from bovine colostrum by means of affinity chromatography on a CDPagarose conjugate. This enzyme forms the sialyl a2+6 galactose linkage according to reaction 5 : CMP-Sia + Galfll+4GlcNAc + Siaa2+6Galfll+4GlcNAc + CMP (5) as first shown by Bartholomew et al. (23) using a partially purified soluble preparation from the same source, During the isolation procedure, the sialyltransferase was conveniently and specifically assayed by quantitating the transfer of [“C] sialic acid from CMP-[l4 C] NeuAc to asialoe, -acid glycoprotein, which contains oligosaccharide chains terminating in the preferred acceptor sequence, Galpl+4GlcNAc.
Introduction The glycosyltransferases comprise a group of enzymes that catalyze the synthesis of specific glycosides by transfer of a monosaccharide from a glycosylnucleotide (nucleotide-sugar) donor substrate to an acceptor substrate as shown in reaction 1: Glycosylnucleotide t acceptor +. Glycosyl-acceptor i- nucleotide (1) The acceptor substrate may be another glycose residue, a polypeptide, or a lipid depending on the specificity of the transferase. UDP-Glucose was the first nucleotide sugar discovered (l), and it was subsequently shown to participate in the synthesis of a complex polysaccharide, following the elucidation of the glycogen synthase reaction (2).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister