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 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 deals researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their software in either the laboratory and undefined. each one quantity within the sequence good points contributions by means of major 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 selection of issues and lengthy ancient pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by means of any scientist drawn to the invention of an enzyme, its homes, and its applications.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
A ganglioside from extraneural tissue has also been reported to contain the Siaa2+6Gal sequence (Table I), but the ability of the colostrum sialyltransferase to utilize glycolipid substrates has not been established. 3. 0-Galactoside a2+3 Sialyltransferase The first of two sialyltransferases to be purified to homogeneity from porcine submaxillary glands (55,71) catalyzes the formation of the Siaa2+ 3Gal linkage according to reaction 6 : CMP-Sia + GalPl+3GalNAc -+ Siacu2+3Gal@l+3GalNAct CMP (6) The acceptor shown is the preferred disaccharide, and this structure serves as an acceptor for the pure sialyltransferase whether is occurs as a free disaccharide, in 0-glycosidic linkage to threonine or serine, or as the nonreducing terminal sequence of glycolipids (Table 1 9 .
The Fuml+4GlcNAc linkage can be quantitated in the presence of the Fucarl+2Gal product using specific fucosidases (89,109). Alternatively, acceptors such as lacto-N-fucopentaose I (Fucc~1+2Gal/31+3GlcNAc/31+3 Galpl+4Glc), which are not acceptors for the a1+2 fucosyltransferases because the 2-hydroxyl on the galactose is already substituted, can be used to assay the a1+4 activity directly (80,90, 115). A branched fucose-containing structure very similar to the Lewis antigen occurs on Type I1 chains which have the nonreducing terminal sequence Gal/31+4GlcNAc.
This activity was only present in the milk of Le(at) individuals and the enzyme was absent from the serum regardless of the Lewis blood type of the donor (109,111). The Leb antigen was subsequently shown to have the nonreducing terminal sequence Fuc~l+2Galfll+3(Fucal+4)GlcNAcfl-(77) and is thus the gene interaction product of the H blood group a1+2 fucosyltransferase and the Lewis blood group a1+4 fucosyltransferase. Except for the human milk enzyme which has been extensively purified (YO), the enzymatic properties of the 0-N-acetylglucosaminide a1+4 fucosyltransferases have not been well characterized.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister