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.
Fluorescence polarization studies on the binding between glutamate dehydrogenase and cytoplasmic aspartate aminotransferase / Salerno, Costantino; J. E., Churchich; P. M., Fasella. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - STAMPA. - 24:6(1975), pp. 351-359.
Fluorescence polarization studies on the binding between glutamate dehydrogenase and cytoplasmic aspartate aminotransferase.
SALERNO, Costantino;
1975
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
