Thyroxine-induced conformational changes in prealbumin
G Irace, H Edelhoch - Biochemistry, 1978 - ACS Publications
G Irace, H Edelhoch
Biochemistry, 1978•ACS PublicationsGaetano Irace* and Harold Edelhoch* abstract: The effects of thyroxine binding on the
conformation of human prealbumin and bovine serum albumin have been examined. A blue
shift in protein absorption was observed with prealbumin, whereas a red shift was observed
with bovine serum albumin. In the case of prealbumin, where the two binding sites are
identical, the total absorption change was confined to the binding of the first ligand and has
been inter-preted as resulting from a conformational change. A blue shift
conformation of human prealbumin and bovine serum albumin have been examined. A blue
shift in protein absorption was observed with prealbumin, whereas a red shift was observed
with bovine serum albumin. In the case of prealbumin, where the two binding sites are
identical, the total absorption change was confined to the binding of the first ligand and has
been inter-preted as resulting from a conformational change. A blue shift
Gaetano Irace* and Harold Edelhoch* abstract: The effects of thyroxine binding on the conformation of human prealbumin and bovine serum albumin have been examined. A blue shift in protein absorption was observed with prealbumin, whereas a red shift was observed with bovine serum albumin. In the case of prealbumin, where the two binding sites are identical, the total absorption change was confined to the binding of the first ligand and has been inter-preted as resulting from a conformational change. A blue shift
ACS Publications