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Inhibition of adenylate kinase by P1,P5-Di(adenosine 5′) pentaphosphate in assays of erythrocyte enzyme activities requiring adenine nucleotides

✍ Scribed by William N. Valentine; Donald E. Paglia; Misae Nakatani; Richard A. Brockway

Publisher: John Wiley and Sons
Year: 1989
Tongue: English
Weight: 191 KB
Volume: 32
Category: Article
ISSN: 0361-8609
DOI: 10.1002/ajh.2830320213

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✦ Synopsis

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 case of hexokinase, phosphofructokinase, and phosphoglycerokinase. In the pyruvate kinase assay, very modest reductions in activity are noted, and kinetics with phosphoenolpyruvate, adenosine diphosphate (ADP), and uridine diphosphate (UDP) are unaltered.

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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 competitiv