Effect of the diazonium salt of sulfanilic acid on human erythrocyte ATPase activity

Masiak, Stanley J.; D'Angelo, Guy

doi:10.1016/0003-9861(73)90503-1

Archives of Biochemistry and Biophysics

1973

DOI: 10.1016/0003-9861(73)90503-1

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Effect of the diazonium salt of sulfanilic acid on human erythrocyte ATPase activity

Stanley J. Masiak

Guy D'Angelo

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1975

1990

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Cited by 2 publications

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“…Early work on the sodium pump reported that acetylation of tyrosine residues of red cell Na,K-ATPase by A-acetylimidazole (NAI)1 produced inactivation of the enzyme (Masiak & D'Angelo, 1973, 1975. The inactivation was prevented by the simultaneous presence of ATP and these workers suggested that an important tyrosine residue was present at the nucleotide binding domain.…”

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N-Acetylimidazole inactivates renal sodium-potassium ATPase by disrupting ATP binding to the catalytic site

Argüello

Kaplan

1990

Biochemistry

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Treatment of renal Na,K-ATPase with N-acetylimidazole (NAI) results in loss of Na,K-ATPase activity. The inactivation kinetics can be described by a model in which two classes of sites are acetylated by NAI. The class I sites are rapidly reacting, the acetylation is prevented by the presence of ATP (K0.5 congruent to 8 microM), and the inactivation is reversed by incubation with hydroxylamine. These data suggest that the class I sites are tyrosine residues at the ATP binding site. The second class of sites are more slowly reacting, not protected by ATP, nor reversed by hydroxylamine treatment. These are probably lysine residues elsewhere in the protein. The associated K-stimulated p-nitrophenylphosphatase activity is inactivated by acetylation of the class II sites only; thus the tyrosine residues associated with ATP binding to the catalytic center are not essential for phosphatase activity. Inactivated enzyme no longer has high-affinity ATP binding associated with the catalytic site, although low-affinity ATP effects (inhibition of phosphatase and deocclusion of Rb) are still present. The inactivated enzyme can still be phosphorylated by Pi, occlude Rb+ ions, and undergo the major conformational transitions between the E1 Na and E2 K forms of the enzyme. Thus acetylation of the Na,K-ATPase by NAI inhibits high-affinity ATP binding to the catalytic center and produces inactivation.

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confidence: 99%

N-Acetylimidazole inactivates renal sodium-potassium ATPase by disrupting ATP binding to the catalytic site

Argüello

Kaplan

1990

Biochemistry

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Effects of N-acetylimidazole on human erythrocyte ATPase Activity. Evidence for a tyrosyl residue at the ATP binding site of the (Na+ + K+)-dependent ATpase

Masiak¹,

D'Angelo²

1975

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Effect of the diazonium salt of sulfanilic acid on human erythrocyte ATPase activity

Cited by 2 publications

References 20 publications

N-Acetylimidazole inactivates renal sodium-potassium ATPase by disrupting ATP binding to the catalytic site

N-Acetylimidazole inactivates renal sodium-potassium ATPase by disrupting ATP binding to the catalytic site

Effects of N-acetylimidazole on human erythrocyte ATPase Activity. Evidence for a tyrosyl residue at the ATP binding site of the (Na+ + K+)-dependent ATpase

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