PMID: 36918Mar 16, 1979

Reversible inactivation of (Na+ + K+)-ATPase by use of a cleavable bifunctional reagent

Biochimica Et Biophysica Acta
J J De Pont


1. Purified (Na+ + K+)-ATPase, prepared from rabbit kidney outer medulla, is incubated with the bifunctional NH2-directed reagent dimethyl 3,3'-dithiobis-propionimidate. This results in a cross-link between the subunits of the enzyme and a simultaneous reduction of the (Na+ + K+)-ATPase and K+-stimulated p-nitrophenylphosphatase activities. 2. The most abundant cross-link product is a dimer of the two different subunits of the enzyme. 3. Reduction of the disulfide cross-link by dithioerythritol results in partial recovery of the original subunit structure of the enzyme and of the (Na+ + K+)-ATPase and K+-stimulated p-nitrophenylphosphatase activities. 4. These results suggest that a free mobility of the subunits of the (Na+ + K+)-ATPase system relative to each other is essential for proper functioning of both enzyme activities.


Aug 1, 1984·Journal of Bioenergetics and Biomembranes·J J De PontS L Bonting


Nov 18, 1975·Biochemistry·S E Hitchcock
Aug 23, 1977·Biochemistry·L O Tack, R T Simpson
Jul 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·G E Davies, G R Stark

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