By Alton Meister
Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative stories of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unequalled view of the old improvement of enzymology. The sequence deals researchers the most recent realizing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic procedure, and their program in either the laboratory and undefined. each one quantity within the sequence positive aspects contributions through major pioneers and investigators within the box from world wide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and similar components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally through any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
A-N-Acetylgalactosaminided + 6 Sialyltransferase A second sialyltransferase to be purified to homogeneity from detergent extracts of porcine submaxillary glands catalyzed reaction 7 : CMP-Sia + CalNAcal+U-Thr/Ser -+ Siaa2+6GalNAcal+O-Thr/Ser + CMP (7) This activity, partially purified from ovine submaxillary glands and first described in the porcine tissue by Carlson et al. (33), is presumed to form the sialylated oligosaccharides of the corresponding submaxillary mucins in viva Sialyltransferase activities that can utilize the GalNAcal+O-ThrlSer substrate to form a different linkage have not been described.
Best disaccharide acceptor was Gal/31+3GalNAc,and other small oligosaccharides were less than 1% as active. , Gal/31+ 4(6)GlcNAc, Gal/31+6GalNAc, Galpl+4Glc) reduces V,, by 15-to 80-fold. With larger oligosaccharides and glycoprotein acceptors, the specificity of GLYCOSY LTRANSFERASES 41 this enzyme was much more strict. The kinetic parameters determined for lacto-N-tetraose are similar to those reported for the corresponding disaccharide, Galpl+3GlcNAc. However, despite the acceptor activity of Nacteyllactosamine (Ga@1+4GlcNAc), lacto-N-neotetraose was not an acceptor at all under conditions sufficient to completely substitute the isomeric lacto-N-tetraose.
A similar structure in which the N-acetylglucosamine residue is replaced by glucose also occurs in human milk oligosaccharides (Table VI). No blood group activity has been firmly established for this structure. Inhibition studies with 3-fucosyllactose have implicated it as the Lewis C antigen on human erythrocytes (1 19), but this has been challenged because of the ubiquity of this structure and the relatively rare occurrence of the Le" antigen on human red cells (I 20). An enzyme that forms the Fuca1+3GlcNAc linkage was first demonstrated in human milk (107).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister