Catalytic properties of the Escherichia coli proton adenosine triphosphatase: evidence that nucleotide bound at noncatalytic sites is not involved in regulation of oxidative phosphorylation-Reference-Cited by-同舟云学术

Catalytic properties of the Escherichia coli proton adenosine triphosphatase: evidence that nucleotide bound at noncatalytic sites is not involved in regulation of oxidative phosphorylation

Published:1985-11-19 Issue:24 Volume:24 Page:6949-6954
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wise John G.,Senior Alan E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00345a030

Reference44 articles.

1. Tightly bound adenine nucleotide in bacterial membrane ATPase

2. The Isolation of Uridine-5'-Triphosphate from Muscle.

3. Paper Chromatography of Nucleoside Polyphosphates.

4. Purification and characterization of the inactive Ca2+, Mg2+-activated adenosine triphosphatase of the unc A− mutant Escherichia coli AN120

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