By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative stories of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the historic improvement of enzymology. The sequence deals researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic procedure, and their program in either the laboratory and undefined. each one quantity within the sequence gains contributions through 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 comparable components of Molecular Biology can be utilized not just by way 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
The enzyme that forms t h s linkage was first detected in porcine liver by Jabbal and Schachter (1 16) with asialo-agalactoa, -acid glycoprotein as acceptor substrate, but the fucose linkage in the product was not established. A similar activity was demonstrated in human serum (1 11,122) and human liver tumors (123). 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.
These and other general features will be considered. The scope of this review is restricted to discussing the glycosyltransferases involved in the biosynthesis of vertebrate, and primarily mammalian glycoconjugates. No attempt will be made to review systematically the Fig. 1. Oligosaccharide structures typically found in glycoconjugates. I, Horse pancreatic ribonuclease (4); 11, human lactoferrin (5); 111, glycophorin (6); IV, porcine submaxillary mucin (6); V, human intestinal glycolipid (7); V1, chondroitin sulfate (6); VII, collagen ( 6 ) .
Since these individuals also completely lack the 0-galactoside a1+2 fucosyltransferase (109,ll l), it was concluded that the H locus encodes the structural gene for this enzyme. Two different approaches have been used to assay the galactoside a1+2 fucosyltransferase in crude preparations where other fucosyltransferases may be present. The first involves the incorporation of fucose from GDPfucose into a nonspecific acceptor such as lactose or asialo-fetuin. The Fucal+2Gal linkage formed can be quantitated directly following destruction of other fucosides with alkali (85,107,l lo), or indirectly by measuring the free fucose released by specific a1+2 fucosidases (89,109).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister