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 experiences of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unequalled view of the historic improvement of enzymology. The sequence bargains researchers the newest knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic procedure, and their program in either the laboratory and undefined. every one quantity within the sequence beneficial properties contributions via best pioneers and investigators within the box from around the globe. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety 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 way of any scientist attracted to the invention of an enzyme, its houses, and its applications.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
The products were characterized to be the gangliosides GM3 and GDla, respectively. Substrate competition and heat inactivation studies suggested that each ganglioside product was formed by a separate enzyme (reactions 3 and 4): I) Ga~l+4Glc-ceramide (lactosylceramide) I CMP-NeuAc Sialyltransferase 1 CMP (3) NeuAccu2+3Calp1+Glc-ceramide (GM3) Galpl+3GalNAc/31+41 Gal0 1+4Glc-ceramide (GM ) NeuAca2+3 ’ CMP-NeuAc CMP Sialyltransferase 2 NeuAca2+3Galp 1+3GalNAc@1+4, Neu Aca293 (4) ’ G a u l +4Glc-ceramide (GD1a) Subsequently these two enzyme activities have been reported in rat liver Colgi apparatus (51), extracts of thyroid glands ( 5 2 ) , and several cultured cell lines (53,54).
6 Enzymic synthesis of this linkage has not been reported. The NeuAca2+6GlcNAc linkage has been reported to occur in the sequence, where R represents a lactosyl group in a human milk oligosaccharide (22) or a mannose residue of a branched asparagine-linked oligosaccharide of bovine prothrombin ( 3 5 ) . The NeuAca2+4GlcNAc linkage has been reported in the Thr/Ser-linked oligosaccharide chains of a rat sublingual glycoprotein (20). To date the enzyme activities synthesizing these linkages have not been identified.
1+ 3)Glc], but in this case, it is the glucose at the reducing end that is substituted (22). It is not known whether the same a1+3 fucosyltransferase is responsible for forming this linkage, and if so, whether the transfer is t o the lactose precursor or to the lacto-N-tetraose. The most common fucose linkage in N-glycosidically linked glycoprotein oligosaccharides is the fucosyl-oll+6 linkage to the asparagine-linked Nacetylglucosamine residue. This structure has been reported in many of the “complex-type’’ oligosaccharide chains in mammalian glycoproteins, but is not observed in the “high mannose-type’’ chains.