Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Escherichia coli adenosine triphosphatase

Bragg, P.D., and Hou, C. (1975) Subunit composition, function, and spatial arrangement in the Ca2+-and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimurium. Arch. Biochem. Biophys. 167, 311-321. [Pg.1050]

Senior, A. E., Richardson, L. V., Baker, K., and Wise, J. G. (1980). Tight divalent cation-binding sites of soluble adenosine triphosphatase (FI) from beef heart mitochondria and Escherichia coli. J. Biol. Chem. 255,7211-7217. [Pg.849]

M Yoshida, N Sone, H Hirata, Y Kagawa and N Ui (1979) Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those of mitochondria, chloroplasts, and Escherichia coli. J Bbl Chem 254 9525-9533... [Pg.733]

Bacterial and Fungal Glycoproteins. — No evidence has been found to substantiate the claim for the presence of covalently-bound carbohydrate in energy-transducing adenosine triphosphatases of Escherichia coli. Incomplete removal of sodium dodecyl sulphate (SDS) after SDS-electrophoresis of the protein results in a positive reaction with the periodate-Schiff staining method. [Pg.313]


See other pages where Escherichia coli adenosine triphosphatase is mentioned: [Pg.273]    [Pg.283]    [Pg.430]    [Pg.347]    [Pg.528]   


SEARCH



Adenosine triphosphatases

Triphosphatase

© 2024 chempedia.info