Title : Inhibition by vanadium of sodium and potassium dependent adenosinetriphosphatase derived from animal and human tissues.

Pub. Date : 1978 Nov-Dec

PMID : 216760






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 In some preparations vanadium was found to be the most potent inhibitor of Na+ + K+ATPase activity so far reported. Vanadium ATPase Na+/K+ transporting subunit beta 1 Homo sapiens
2 Concentrations of vanadium causing 50 percent inhibition of Na+ + K+ATPase activity ranged from 6 x 10(-8) to 5 x 10(-7) M in microsomal fractions and from 2 x 10(-7) to 1 x 10(-6) M in tissue homogenates. Vanadium ATPase Na+/K+ transporting subunit beta 1 Homo sapiens
3 Mg2+ ATPase, which contaminated the enzyme preparations to a variable degree, was 1,000-10,000 times more resistant to vanadium than was Na+ + K+ATPase. Vanadium ATPase Na+/K+ transporting subunit beta 1 Homo sapiens
4 This could mean that vanadium inhibits the Na+ + K+ATPase at the site activated by Na+, and that ATP protects the enzyme either by binding vanadium or by competing for a mutual receptor on the enzyme. Vanadium ATPase Na+/K+ transporting subunit beta 1 Homo sapiens