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, supplying an unequalled view of the old improvement of enzymology. The sequence deals researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their program in either the laboratory and undefined. each one quantity within the sequence gains contributions by way of major pioneers and investigators within the box from worldwide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of issues and lengthy historic pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally via any scientist attracted to the invention of an enzyme, its homes, and its applications.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62
Under certain circumstances, however, y-glutamyltransferase activity may not reflect the biosynthetic activity of the enzyme (15). The biosynthetic activity can also be assayed calorimetrically by substituting NH20H for NH3 in Reaction (1). A. AMINO ACID SEQUENCE AND MOLECULAR STRUCTURE The amino acid sequence of the E. coli GS obtained by the DNA sequencing method has been reported (1 1) and is given in Table 1. The amino acid composition obtained from the sequence data is in reasonable agreement with that reported earlier (2).
Biol. Chem. 251, 7709 (1976). 49. , J. Mol. Biol. 190, 163 (1986). 50. , Baer, M. , J . Mol. , in press. 51. , Nishikawa, S . , EMBO J. 5, 1697 (1986). 52. , personal communication. 53. , Mol. Cell. Biol. 6 , 1058 (1986). 54. , J . Biol. Chem. 260,5942 (1985). 55. S. , Cell 44, 213 (1986). 56. , Cell 44, 225 (1986). 36 SIDNEY ALTMAN 57. , in Subviral Pathogens of Plants and Animals: Viroids and Prions (K. J. ), pp. 235-263, Academic Press, New York (1985). 58. , Science 223,450 (1984). 59. , Biochemistry 24, 4785 (1985).
Separation by the antibody method was based on the observation that antibody directed against AMP-bovine serum albumin conjugate exhibits high affinity for the AMP moiety of adenylylated glutamine synthetase as well as for AMP (50), which can be used to elute the antibody-bound enzyme. The polyclonal anti-AMP antibody column separates fully adenylylated enzyme from fully unadenylylated enzyme, but it fails to separate the mixture of partially adenylylated enzyme forms. This procedure was improved by using different monoclonal antibody columns, particularly that of IgG and of IgM because IgG exhibits higher affinity for AMP moiety than does IgM, yet IgG consists of two binding sites while IgM possesses 10 sites.