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By Alton Meister

Advances in Enzymology and similar components 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 historic improvement of enzymology. The sequence deals researchers the most recent realizing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their software in either the laboratory and undefined. each one quantity within the sequence positive factors contributions by way of top 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 historic 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 via any scientist attracted to the invention of an enzyme, its houses, and its applications.

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Cone, J. , and Stadtman, T. ,J. Bzol. , 252, 53375344 (1977). 53. Rotruck, J. , Pope, A. , Ganther, H. , Swanson, A. , Hafeman, D. , and Hoekstra, W. , Science, 179, 588-590 (1973). 54. , Biochem. Biophys. Acta, 358, 251261 (1974). 55. , Giinzler, W. , and Schock, H. , 32, 132-134 (1973). 56. Mills, G. , and Randall, H. J. Biol. , 232, 589-598 (1958). 57. O’Brien, P. , and Little, C. Can. J . , 47, 493 (1969). 58. , and Giinzler, W. A, in Glutathione, W. B. , Academic Press, New York, 1974, pp.

41. , Huang, J. J. , Biochem. Biophy. Acta, 336, 427-436 (1974). 42. Orme-Johnson, W. , and Hansen, R. , Tsibris, J. C. , Bartholomaus, R. , and Gunsalus, I. , Proc. Natl. Acad. Sci. U S . , 60, 368372 (1968). 43. , and Chan, W. , J. Am. Chem. ,89, 3892-3898 (1967). 44. Pal, B. , and Schmidt, D. , J. Am. Chem. , 99, 1973-1974 (1977). 45. Giinther, W. H. , and Mautner, H. ,J. Am. Chem. ,87, 2708-2716 (1965). 46. , 2033-2036 (1976). 47. Giinther, W. H. , and Mautner, H. , cited as personal communication on p.

The endoglycosidase from Diplococcus pneumoniae, designated endo-P-N-acetylglucosaminidase D (39), will hydrolyse only oligosaccharides of type 2 (Fig. l), in which the Man-a(1+3) moiety is not substituted (93); R'" in compounds of R' Man a (146) R" Man a (1+3) \ Man /3 (1-4) / GlcNAc /3 ( 1 4 4 ) GlcNAc p (I-tN) Asn 1 R"' Man a (1+6) Man (Y (1+3) \ / Man /3 (1+4) GlcNAc /3 (1-+4) GlcNAc /3 (I+N) Asn 2 Man /3 (1-t4) GlcNAc p (1+4) GlcNAc (1+N) Asn 3 GlcNAc /3 (1+N) Asn 4 Fig. 1. Substrates for endo-/3-N-acetylglucosaminidases(compounds 1, 2, and 3), and common product of digestion of these substrates by the enzymes (compound 4).

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