Fluorescence polarization studies on the binding between glutamate dehydrogenase and cytoplasmic aspartate aminotransferase

Autor:	C, Salerno, J E, Churchich, P M, Fasella
Jazyk:	angličtina
Rok vydání:	1975
Předmět:	Binding Sites Cytosol Spectrometry Fluorescence Glutamate Dehydrogenase Swine Myocardium Animals Cattle Serum Albumin Bovine Aspartate Aminotransferases Hydrogen-Ion Concentration Protein Binding
Popis:	Polarization of fluorescence measurements on aspartate aminotransferase (from pig heart cytosol) labeled with fluorescein isothiocyanate have been used to detect the formation of a soluble complex of this protein wich glutamate dehydrogenase from bovine liver. The binding of the labeled transaminase to dehydrogenase is detectable at catalytic concentrations of the enzymes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::944a5ae3483ed5c1e10bbccb7942a279 http://hdl.handle.net/11573/465367 Zobrazit plný text záznamu