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Secretin: specific binding to rat brain membranes

Journal Article · · J. Neurosci.; (United States)
OSTI ID:5478113
The binding of (/sup 125/I)secretin to rat brain membranes was investigated. Radiolabeled secretin bound with high affinity (KD . 0.2 nM) to a single class of noninteracting sites. Binding was specific, saturable, and reversible. Regional distribution studies indicated that the specific binding was greatest in the cerebellum, intermediate in the cortex, thalamus, striatum, hippocampus, and hypothalamus, and lowest in the midbrain and medulla/pons. Pharmacological studies indicated that only secretin, but not other peptides, inhibits binding of (/sup 125/I)secretin with high affinity. Also, certain guanine nucleotides inhibited high affinity binding. These data indicate that rat brain membranes possess high affinity binding sites specific for secretin and that with the use of (/sup 125/I) secretin the kinetics, stoichiometry, specificity, and distribution of secretin receptors can be directly investigated.
Research Organization:
Department of Biochemistry, George Washington University School of Medicine and Health Sciences, Washington, DC
OSTI ID:
5478113
Journal Information:
J. Neurosci.; (United States), Journal Name: J. Neurosci.; (United States) Vol. 3:8; ISSN JNRSD
Country of Publication:
United States
Language:
English

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