A difference in the affinity labeling of Ca2+, Mg2+-activated ATPases of normal and unc A strains of Escherichiacoli by the 2′,3′-dialdehyde derivative of adenosine 5′-diphosphate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Membrane Adenosine Triphosphatases of Prokaryotic Cells
2. The uncA gene codes for the α-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains
3. Properties of membranes from mutant strains of Escherichia coli in which the β-subunit of the adenosine triphosphatase is abnormal
4. Pyruvate Carboxylase Affinity Labelling of the Magnesium Adenosine Triphosphate Binding Site
5. Affinity labeling of bovine colostrum galactosyltransferase with a uridine 5'-diphosphate derivative
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1. Studies on the active site of the Neurospora crassa plasma membrane H+-ATPase with periodate-oxidized nucleotides;Journal of Biological Chemistry;1989-07
2. Kinetics of protein modification reactions: interpretation of reaction order;Journal of Molecular Catalysis;1986-02
3. Loss of protection by nucleotides against proteolysis and thiol modification in the isolated α-subunit from F1 ATPase of Escherichia coli mutant uncA401;Biochemical Journal;1984-11-15
4. The ATPase complex of Escherichia coli;Canadian Journal of Biochemistry and Cell Biology;1984-11-01
5. Precautions when determining kinetically the order of inactivation of enzymes by functionally irreversible inhibitors;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1984-09
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