Interaction of rabbit muscle enolase and 3-phosphoglycerate mutase studied by ELISA and by batch gel filtration.

TitleInteraction of rabbit muscle enolase and 3-phosphoglycerate mutase studied by ELISA and by batch gel filtration.
Publication TypeJournal Article
Year of Publication1992
AuthorsNazaryan, K. B., F. Climent, S. Simonian, P. Tompa, and J. Batke
JournalArch Biochem Biophys
Volume296
Issue2
Pagination650-3
Date Published1992 Aug 1
ISSN0003-9861
KeywordsAnimals, Brain, Cattle, Chromatography, Gel, Enzyme-Linked Immunosorbent Assay, Fluorescein-5-isothiocyanate, Fluorescence Polarization, Fluorescent Dyes, Macromolecular Substances, Muscles, Phosphoglycerate Mutase, Phosphopyruvate Hydratase, Rabbits
Abstract

The interaction of rabbit skeletal muscle enolase and 3-phosphoglycerate mutase was detected by an ELISA test, a batch gel-filtration technique, and fluorescence anisotropy measurements, and the activity of enolase was determined to be a function of mutase concentration. The apparent dissociation constant of this enzyme complex is approximately 1 microM. This value seems to be independent of the presence (in fluorescence anisotropy measurements) or the absence (in activity as well as in ELISA experiments) of fluorescein isothiocyanate used widely as a label for determining the complex formation between enzymes in fluorescence anisotropy measurements.

Alternate JournalArch. Biochem. Biophys.
PubMed ID1321593