Download PDF by Alton Meister: Advances in Enzymology and Related Areas of Molecular

By Alton Meister

ISBN-10: 0470122978

ISBN-13: 9780470122976

ISBN-10: 0471081205

ISBN-13: 9780471081203

Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative studies of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the old improvement of enzymology. The sequence deals researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their program in either the laboratory and undefined. every one quantity within the sequence gains contributions by means of prime pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.

With its wide selection of issues and lengthy old pedigree, Advances in Enzymology and comparable parts 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 homes, and its applications.

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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52

Example text

The substrate specificity of the a1+6 fucosyltransferase was elucidated by Wilson et al. (93). It had previously been assumed that fucose was added by the enzyme to the terminal P-N-acetylglucosamine in asialo- GLYCOSYLTRANSFERASES 51 agalactoal,-acid glycoprotein; however, after treatment of the product with an endog-N-acetylglucosaminidasethat cleaves between the two N-acetylglucosamine residues in the chitobiose core, the fucose remained bound to the asparagine-linked N-acetylglucosamine residue rather than to the released oligosaccharide.

38 BEYER, SADLER, REARICK, PAULSON, A N D HILL While the primary role of the P-galactoside a2+6 sialyltransferase in vivo may be to sialylate the nonreducing terminal GaUlj4GlcNAc sequence of complex asparagine-linked oligosaccharides, other glycosyltransferases can utilize the same sequence and thus provide alternate biosynthetic patterns of glycosylation (Section 111). Of particular interest is the evidence from structural studies that different branches of the same asparagine linked oligosaccharide may contain sialic acid in both a2+6 and a2+3 linkages (4,35,67).

Of only certain individuals, termed secreto or^" (77). An enzymic basis for secretor status was shown by Shen et al. (107), who demonstrated that the P-galactoside a1+2 fucosyltransferase was absent from the milk of nonsecretors. Chester and Watkins (89) subsequently demonstrated that the enzyme was also absent in the submaxillary glands and gastric mucosa of nonsecretors. In contrast, the enzyme was present in the serum (109,111) and the bone marrow (110) of all individuals except those of Bombay phenotype, regardless of secretor status.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister

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