Download e-book for kindle: Advances in Enzymology and Related Areas of Molecular by Alton Meister

By Alton Meister

ISBN-10: 0470123117

ISBN-13: 9780470123119

ISBN-10: 0471527602

ISBN-13: 9780471527602

Site visitors ATPases: A Superfamily of delivery Proteins working from Escherichia coli to people (G. Ames, et al.).

The respiration Burst Oxidase (B. Babior).

seasoned- and Antioxidant capabilities of Quinones and Quinone Reductase in Mammalian Cells (E. Cadenas & P. Hochstein).

The Redox facilities of Ribonucleotide Reductase of Escherichia coli (M. Fontecave, et al.).

lengthy variety Intramolecular associated features within the Calcium delivery ATPase (G. Inesi, et al.).

Hydrogen-Bonding in Carbohydrates and Hydrate Inclusion Compounds (G. Jeffrey).

Methylation of mRNA (P. Narayan & F. Rottman).

Mammalian Nitric Oxide Synthases (D. Stuehr & O. Griffith).

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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 65

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Chem. 266, 8946-8951. Dean, D. , Fikes, J. , Bassford, P. J. , and Nikaido, H. (1989). Active transport of maltose in membrane vesicles obtained from Escherichia coli cells producing tethered maltose-binding protein, J. , 171, 503-5 10. Doolittle, R. , Johnson, M. , Houten, B. , Thomas, D. , and Sancar, A. (1986). Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins, Nature (London), 323, 451 -453. Dreusicke, D . , Karplus, A , , and Schultz, G.

5451. Ames, G. , Groarke, J. and Petithory, J . (1989). Reconstitution of periplasmic transport in inside-out membrane vesicles: Energization by ATP, J . Biol. , 264, 3998-4002. TRAFFIC ATPacs 43 Ames, G. -L. and Spudich, E. N . (1976). Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein Proc. Nutl. Acad. S C ~USA, . 73, 1877-1881. Anderson, M. , Berger, H. , Rich, D. , Gregory, R. J . , Smith, A. , and Welsh, M. J. Nucleoside triphosphates are required to open a CFTR chloride channel.

Does the ATP-binding activity of HisQ exhibit any such limitations? Several experiments to answer these questions were performed with genetically constructed strains lacking one or another of the membrane components (Shyamala, Baichwal, and Ames, in preparation). Membranes from strains lacking HisQ were tested for the ability of HisP to bind ATP and shown to lack such activity completely. This can be interpreted to mean that in order to be able to bind ATP, HisP either needs to be assembled within a complex, or to be exposed to HisQ at some time during its lifetime.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 65 by Alton Meister


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