Polypeptide Hormone Interaction
Year: 1972
Type: article
Abstract: The binding of glucagon to lysolecithin has been evaluated by fluorescence techniques. Fluorescence spectra and polarization measurements indicate that the hormone is bound to lysolecithin micelles. Since the rate of micelle dissociation below its critical micelle concentration is rather slow, binding is observed at all concentrations of lysolecithin. By similar criteria, the polypeptide hormone calcitonin, but not adrenocorticotropic hormone, was bound to lysolecithin micelles. Phosphatidyl serine showed very weak binding and lecithin no binding of glucagon. The colloidal properties of lysolecithin were evaluated from its interactions with two fluorescent dyes, i.e. eosin and 8-anilino-1-naphthalene sulfonate.
Source: Journal of Biological Chemistry
Authors: Arthur B. Schneider, Harold Edelhoch
Institution: National Institutes of Health
Language: French
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1572237609