Title | Interaction of rabbit muscle enolase and 3-phosphoglycerate mutase studied by ELISA and by batch gel filtration. |
Publication Type | Journal Article |
Year of Publication | 1992 |
Authors | Nazaryan, K. B., F. Climent, S. Simonian, P. Tompa, and J. Batke |
Journal | Arch Biochem Biophys |
Volume | 296 |
Issue | 2 |
Pagination | 650-3 |
Date Published | 1992 Aug 1 |
ISSN | 0003-9861 |
Keywords | Animals, 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 Journal | Arch. Biochem. Biophys. |
PubMed ID | 1321593 |
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