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 studies of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unmatched view of the historic improvement of enzymology. The sequence deals researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in complicated organic technique, and their program in either the laboratory and undefined. every one quantity within the sequence beneficial properties contributions by means of major 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 variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally through any scientist attracted to the invention of an enzyme, its homes, and its applications.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 48
GLYCOSIDASES 33 Finally, we turn to the physical and biological effects of glycosidases on cells as mediated by their action on cell-surface saccharide components. 11. Isolation and Purification The classical methods of isolation of proteins, including differential solubilities, binding to adsorbents and ion exchangers, and crystallization, have all been applied to glycosidases, but only a limited number of these enzymes had been purified until recently. These methods are usually laborious and require processing of large volumes containing only small amounts of the desired enzyme.
Arch. B i o c h . , 99, 36-44 (1962). 94. Stadtman, T. , J. Biol. , 231, 961-973 (1958). 95. Stadtman, T . , Arch. Biochem. , 113, 9-19 (1966). 96. , and Stadtman, T . , unpublished data. 28 THRESSA C. STADTMAN 97. Brown, N. , Canellakis, Z. , and Thelander, L. J. , 9, 561-573 (1969). 98. ,J. Biol. C h . ,249, 4858-4862 (1974). 99. Atkin, C. , J. Biol. , 248, 7464-7472 (1973). 100. Reichard, P. Fed. , 37, 9-14 (1978). 101. , and Stadtman, T. , unpublished data. 102. Stadtman, T. , unpublished data.
However, there have recently been a number of interesting examples of glycosidases that cleave selectively, or specifically, one or more of such linkages. Two a-L-fucosidases were isolated from Trichomonasfoetus, one of which was specific for (1+2)-linkages and destroyed the H-activity of a blood-group active glycoprotein, while the other hydrolyzed L-fucopyranosyl-a(1-3) and a(1-+4)-N-acetylglucosamineand destroyed L e a activity; it did not hydrolyze L-fucopyranosyl a(1-6) N-acetylglucosamine (92).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 48 by Alton Meister