Characterization of ATP-diphosphohydrolase from rat mammary gland

ATP-diphosphohydrolase (or apyrase) hydrolyses nucleoside di- and triphosphates in the presence of millimolar concentration of divalent cations. It is insensitive towards sulfhydryl and aliphatic hydroxyl-selective reagents and to specific inhibitors of ATPases. We present further evidence that ATPa...

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Published in:The international journal of biochemistry & cell biology 1996, Vol.28 (1), p.75-79
Main Authors: Alvarez, A., Chayet, L., Galleguillos, M., García, L., Kettlun, A.M., Collados, L., Traverso-Cori, A., Mancilla, M., Valenzuela, M.A
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - antagonists & inhibitors
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Animals
Apyrase - antagonists & inhibitors
Apyrase - chemistry
Apyrase - metabolism
Apyrose
ATP-diphosphohydrolase
Binding, Competitive
Female
Kinetics
Mammary gland
Mammary Glands, Animal - enzymology
Rats
Rats, Sprague-Dawley
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Summary:ATP-diphosphohydrolase (or apyrase) hydrolyses nucleoside di- and triphosphates in the presence of millimolar concentration of divalent cations. It is insensitive towards sulfhydryl and aliphatic hydroxyl-selective reagents and to specific inhibitors of ATPases. We present further evidence that ATPase and ADPase activities present in rat mammary gland correspond to apyrase. Two kinetic approaches have been employed, competition plot and chemical modification with group-selective reagents. The M r of these activities was determined by 60Co radiation-inactivation. The kinetic approaches employed, competition plot (which discriminate whether competitive reactions occur at the same site) and chemical modification, point to the presence of a single protein which hydrolyses ATP and ADP. The similar M r values of ATPase and ADPase activities also support this proposal. ATPase and ADPase activities of mammary gland show a similar sensitivity or insensitivity towards several chemical modifiers. These results suggest that this enzyme is ATP-diphosphohydrolase, also known as apyrase. The results obtained are compared with the ones obtained by us and other authors with the enzyme isolated from other sources.
ISSN:1357-2725
1878-5875
DOI:10.1016/1357-2725(95)00114-X