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By Alton Meister

Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, providing researchers entry to authoritative reports of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the old improvement of enzymology. The sequence bargains researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic method, and their program in either the laboratory and undefined. each one quantity within the sequence good points contributions by means of top pioneers and investigators within the box from all over the world. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.

With its wide variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition through any scientist attracted to the invention of an enzyme, its houses, and its applications.

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Sample text

The substrate specificity of this transferase suggests that it must act after the addition of terminal N-acetylglucosamine residues, during the synthesis of the complex-type and high mannose-type oligosaccharides (93), but before the addition of the peripheral galactose, sialic acid, and fucose residues. Thus the attachment of the fucose may play some regulatory role in the synthesis of the terminal sequences in the complex-type chains. ). Fucosyltransferase activities capable of forming the other fucose linkages shown in Table VI have not been demonstrated.

Further purification of the 0-galactoside a2+3 sialyltransferase was achieved by specific elution from a third column of CDP-agarose with a CTP gradient. The enzyme was brought to homogeneity and separated into two noninterconverting forms with different Stokes radii by a final gel fitration chromatography on Sephadex G-200. 6 pmole product formed per minute per milligram enzyme using the best known acceptor, antifreeze glycoprotein. In a typical purification, two-thirds of the enzyme was isolated as form A (Stokes radius 51 A) and one-third as form €3 (Stokes radius 31 A).

Thus a single sialyltransferase may account for the biosynthesis of the Siaa2+3Ga@lQGalNAcal+ 0-ThrlSer sequences of glycoproteins as well as the Siaa2+3Gal linkages to the galactose residue distal to the ceramide moiety of gangliosides such as GDla: , , Siaa2+3Galpl+3GalNAcP1+4 /Galpl+4Glc+Cer Siaa2+3 As suggested earlier (27), a separate enzyme is needed to attach the sialic acid to the proximal galactose. In addition, the porcine enzyme cannot form the Siaa2+3Gal~l+4GlcNAcsequence that has been reported in the asparagine-linked oligosaccharides of several glycoproteins (4,6,35,67,73).

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