By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative reports of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the old improvement of enzymology. The sequence deals researchers the newest figuring out 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 beneficial properties contributions via best pioneers and investigators within the box from worldwide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety of themes and lengthy historic pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just by way of scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition 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
The use o f glycosyltransferases in the structure-finction analysis o f oligosaccharides. Several glycosyltransferases have been shown to be very valuable reagents for modifying oligosaccharide structures. Because of their strict acceptor specificities, simply determining whether an oligosaccharide is an acceptor for a particular transferase may give valuable structural information. Moreover, they may also be used effectively, often in conjunction with glycosidases, for structural analysis as well as for determining oligosaccharide structure-function relationships, particularly oligosaccharides on cell surfaces.
6 pmole product formed per minute per milligram enzyme using the best known acceptor, antifreeze glycoprotein. In a typical purification, two-thirds of the enzyme was isolated as form A (Stokes radius 51 A) and one-third as form €3 (Stokes radius 31 A). Both forms of the enzyme were subsequently found to exhibit identical enzymic properties and were homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis with similar polypeptide molecular weights of about 50,000. The molecular basis for the separation of the two forms of the enzyme by gel filtration appears to be the binding of nearly an equal weight of Triton X-100 by form A to give a complex with an apparent molecular weight of 106,000 (55,72).
At saturating substrate concentrations, both acceptors were equally effective as indicated by similar values for Vma. 93 mM), suggesting that in vivo the GalP1~3GalNAca1+0-Thr/Serstructure may be sialylated in preference to the GalNAcal+O-ThrlSer structure if substrate concentrations are less than saturating. Alternatively, these observations might be explained as an effect on sialyltransferase activity due to the different polypeptide structures of the substrates. Initial rate and inhlbition studies with these acceptors indicated that the mucin sialyltransferase has either a random sequential (equilibrium) kinetic mechanism or an ordered sequential (steady-state) mechanism in which the donor substrate binds first.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 52 by Alton Meister