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 parts of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unmatched view of the historic improvement of enzymology. The sequence bargains researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic approach, and their program in either the laboratory and undefined. each one quantity within the sequence beneficial properties contributions by way 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 themes and lengthy old pedigree, Advances in Enzymology and similar components of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by way of any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
The glycosidic linkage synthesized by the pure enzyme has been determined using the substrates, lactose, Galpl+3GalNAc, and antifreeze glycoprotein. The latter protein contains the disaccharide, Calp1+3GalNAc, in glycosidic linkage to threonine (74). In each case the composition, the paper chromatographic properties, and the stability to periodate oxidation of the product were consistent with the product structure, Siaa2+3Gal (25). The kinetic properties of the P-galactoside a2+3 sialyltransferase have been investigated by initial rate and inhibition studies.
It catalyzed the synthesis of 2’-fucosyllactose (Fucal+2Ga431+4Glc) from lactose and GDP-fucose. The structure of the product was inferred from its alkaline stability, a unique property of fucosyl a1+2 galactosides (105). This fucosyltransferase activity has subsequently been demonstrated in hog gastric mucosa (106), HeLa cells (79), human milk (107), human submaxillary gland and stomach mucosa (89), rat small intestinal mucosa (108), porcine submaxillary glands (76), human serum (109), human bone marrow (1 lo), and bovine spleen (82).
The combined and sequential actions of many transferases could lead to the Synthesis of a variety of oligosaccharide structures, but because of the rigid acceptor substrate specificities of the transferases, synthesis of only certain oligosaccharides is permitted. In some cases, it is now possible to deduce how the combined actions of these enzymes lead to the synthesis of well-known structures found in either 0-or N-linked oligosaccharides of glycoproteins. 3. The use o f glycosyltransferases in the structure-finction analysis o f oligosaccharides.