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Measurement of mitochondrial oxidative phosphorylation: Selective inhibition of adenylate kinase activity by P1,P5-di-(adenosine-5′)-pentaphosphate

✍ Scribed by Ronald L. Melnick; Charles P. Rubenstein; Shirley M. Motzkin

Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
441 KB
Volume
96
Category
Article
ISSN
0003-2697

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✦ Synopsis

A biochemical assay for the measurement of ATP synthesis coupled to electron transport in the presence of adenylate kinase was developed as an alternative to using the conventional Clark-type oxygen electrode. The assay utilizes Pi,p-di-(adenosine-5')-pentaphosphate which is shown to he a competitive inhibitor with MgADP for rat liver mitochondrial adenylate kinase (Xi = 7.04 x IO-* M) and was found to have no effect on oxidative phosphorylation of either intact mitochondria or submitochondrial particles,

METHODS

Mitochondria

were isolated fresh daily from the livers of 150-g male albino rats of the CD strain (Charles River Breeding Laboratories, Wilmington, Mass.) as de-1

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Inhibition of adenylate kinase by P1,P5-
Inhibition of adenylate kinase by P1,P5-Di(adenosine 5′) pentaphosphate in assays of erythrocyte enzyme activities requiring adenine nucleotides
✍ William N. Valentine; Donald E. Paglia; Misae Nakatani; Richard A. Brockway 📂 Article 📅 1989 🏛 John Wiley and Sons 🌐 English ⚖ 191 KB

P1,P5-di(adenosine 5')pentaphosphate (Ap5A) is an excellent inhibitor of human hemolysate adenylate kinase at concentrations near 2 microM and above. At ten times this concentration and in hemolysate enzyme assays under conditions described in this paper it appears not to alter reaction data in the