Fluorescent modification of adenosine 3′,5′-monophosphate: Spectroscopic properties and activity in enzyme systems

John A. Secrist, Jorge R. Barrio, Nelson J. Leonard, Carlos Villar-Palasi, Alfred G. Gilman

Research output: Contribution to journalArticle

56 Scopus citations

Abstract

The synthesis of a highly fluorescent analog of adenosine 3′,5′-monophosphate, namely, 1,N6-ethenoadenosine 3′,5′-monophosphate, has provided a powerful probe for systems involving adenosine 3′,5′-nonophosphate. The potential utility of this analog is indicated by its long flouorescent lifetime, detectability at low concentration, and relatively long wavelength of excitation (300 nanometers). In protein kinase systems it is a highly acceptable substitute for adenosine 3′,5′-monophosphate.

Original languageEnglish (US)
Pages (from-to)279-280
Number of pages2
JournalScience
Volume177
Issue number4045
DOIs
StatePublished - Jan 1 1972

ASJC Scopus subject areas

  • General

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    Secrist, J. A., Barrio, J. R., Leonard, N. J., Villar-Palasi, C., & Gilman, A. G. (1972). Fluorescent modification of adenosine 3′,5′-monophosphate: Spectroscopic properties and activity in enzyme systems. Science, 177(4045), 279-280. https://doi.org/10.1126/science.177.4045.279