Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/11061
Title: Specific binding of D-Tyr25 (Nle28,31)-CCK(25-33) to cortical membranes from rat brain.
Authors: Carlberg, M;Jarrott, B;Beart, P M
Affiliation: University of Melbourne, Clinical Pharmacology and Therapeutics Unit, Austin Hospital, Heidelberg, Vic.
Issue Date: 14-Jan-1991
Citation: Neuroscience Letters; 122(1): 29-32
Abstract: The 125I-labeled sulfonated cholecystokinin (CCK) analogue, D-Tyr25(Nle28,31)-CCK(25-33), bound saturably and reversibly to membranes of rat cerebral cortex. The dissociation constant Kd was estimated to be 0.14 nM by Scatchard analysis and 0.40 nM from analyses of dissociation/association rates. Hill coefficients of 0.99, Scatchard plots and drug competition studies were consistent with a single population of binding sites. Dependence on divalent cations and inhibition by guanylyl-imidodiphosphate suggested binding to a receptor coupled to a G protein. Competition studies with CCK-analogues and non-peptide specific antagonists indicated binding to receptor sites of the B-subtype (CCKB).
Internal ID Number: 2057133
URI: http://ahro.austin.org.au/austinjspui/handle/1/11061
URL: http://www.ncbi.nlm.nih.gov/pubmed/2057133
Type: Journal Article
Subjects: Animals
Benzodiazepinones.metabolism
Binding, Competitive
Cerebral Cortex.metabolism
Cholecystokinin.analogs & derivatives.metabolism
Half-Life
In Vitro Techniques
Iodine Radioisotopes.diagnostic use
Kinetics
Male
Membranes.metabolism
Peptide Fragments.metabolism
Phenylurea Compounds
Rats
Rats, Inbred Strains
Receptors, Cholecystokinin.antagonists & inhibitors.metabolism
Appears in Collections:Journal articles

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