By Alton Meister
Advances in Enzymology and comparable parts of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative studies of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the ancient improvement of enzymology. The sequence deals researchers the most recent realizing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic approach, and their software in either the laboratory and undefined. every one quantity within the sequence positive factors contributions by way of best pioneers and investigators within the box from world wide. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy old 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 via any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 48
Their activity towards more complex saccharides, including glycoproteins and glycolipids, is generally considerably reduced and is often completely absent. Since activity may vary depending on the source of the enzyme, it is desirable to obtain glycosidases with different properties from a wide variety of sources such as mammalian organs, invertebrates, higher plants, molds and bacteria. 111. Substrates A. SPECIFICITY Various types of specificity have been defined in the action of glycosidases.
74. , personal communication. 74a. Tappel, A. L, Forstrom, J. , Zakowski, J. , Lyons, D. , and Hawkes, W. C . , Fed. , 37, 706 (1978). 75. Prohaska, J. , Hoekstra, W. , and Ganther, H. , Biochem. Biophys. Res. , 74, 64-71 (1977). 76. Cone, J. , Davis, J. , and Stadtrnan, T. , Proc. Natl. Acad. Sci. U S . , 73, 2659-2663 (1976). 77. Whanger, P. , Pedersen, N. , and Weswig, P. , Biochem. Biophys. Res. , 53, 1031-1035 (1973). 78. , B i 0 c h . J . 57, 10-16 (1954). 79. Lester, R. L. and De Moss J.
GLYCOSIDASES 41 type 2 may be of the same structure as R’ and Rrrin compounds of type 1. perfringens (38b). A third type of enzyme of this group, endo-P-N-acetylglucosaminidaseL, is present in S. griseus, (38a); it acts on the asparaginyl trisaccharide 3 (Fig. 1) hydrolysing it to the disaccharide Man+( 1+4)-GIcNAc and N-acetylgIucosaminy1L-asparagine (compound 4, Fig. 1). The latter is also the product of hydrolysis of the more complex asparaginyl carbohydrates 1 and 2 by the other endoglycosidases, H and D.
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