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An enzymatic method for inosine 5′-monophosphate in the femtomole range

✍ Scribed by Douglas A. Young; Joyce A. Carter; Maggie M.-Y. Chi; Oliver H. Lowry

Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
376 KB
Volume
134
Category
Article
ISSN
0003-2697

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✦ Synopsis

A method for measuring inosine 5'-monophosphate (IMP) by enzymatic generation of NADPH is described. Procedures are given for direct fluorometric assay in the nanomole range and indirect measurement with amplification by enzymatic cycling in the pico- and femtomole ranges. The most sensitive procedure represents a nearly 50,000-fold increase in sensitivity over enzymatic methods now available. Specificity of the assay was greatly enhanced by the use of the antibiotic coformycin, a potent inhibitor of adenosine deaminase (EC 3.5.4.4). This enzyme was found to be a major contaminant of one of the necessary enzymes, phosphoglucomutase (EC 2.7.5.1). The use of the method is illustrated by measurements of IMP in single stimulated and control rat muscle fibers.

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