Fluorescent modification of adenosine 3',5'-monophosphate: spectroscopic properties and activity in enzyme systems.

Science (New York, N.Y.) ·Vol. 177 ·No. 4045 ·1972-07-21 ·Pages 279-80

Secrist JA, Barrio JR, Leonard NJ, Villar-Palasi C, Gilman AG

Abstract

The synthesis of a highly fluorescent analog of adenosine 3',5'-monophosphate, namely, 1,N(6)-ethenoadenosine 3',5'-monophosphate, has provided a powerful probe for systems involving adenosine 3',5'-monophosphate. The potential utility of this analog is indicated by its long fluorescent 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.

MeSH Terms

Acetaldehyde Acetals Adenosine Triphosphate Animals Cattle Chemical Phenomena Chemistry Chlorine Chromatography, Thin Layer Cyclic AMP/chemical synthesis Enzyme Activation Fluorescence Imidazoles/chemical synthesis Muscles/enzymology Myocardium/enzymology Phosphoric Diester Hydrolases Phosphorus Isotopes Phosphotransferases Protein Binding Proteins Rabbits Spectrophotometry Structure-Activity Relationship Tritium Ultraviolet Rays

Chemicals

Acetals Imidazoles Phosphorus Isotopes Proteins Tritium 1,N(6)-ethenoadenosine 3',5'-monophosphate Chlorine Adenosine Triphosphate Cyclic AMP Phosphotransferases Phosphoric Diester Hydrolases Acetaldehyde

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Secrist J A

Barrio J R

Leonard N J

Villar-Palasi C

Gilman A G

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.177.4045.279

Published

1972-07-21

Pages

279-80

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.177.4045.279 View journal details

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Fluorescent modification of adenosine 3',5'-monophosphate: spectroscopic properties and activity in enzyme systems.

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