1. Localization of [3H]glutamate binding sites in rat adrenal medulla
- Author
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Kiyokazu Ogita and Yukio Yoneda
- Subjects
Male ,medicine.medical_specialty ,N-Methylaspartate ,Glutamic Acid ,Acetates ,Binding, Competitive ,chemistry.chemical_compound ,Glutamates ,Internal medicine ,Medullary part ,medicine ,Animals ,Quisqualic acid ,Molecular Biology ,Acetic Acid ,Cerebral Cortex ,Aspartic Acid ,Oxadiazoles ,Binding Sites ,General Neuroscience ,Quisqualic Acid ,Rats, Inbred Strains ,Glutamate binding ,In vitro ,Rats ,medicine.anatomical_structure ,Endocrinology ,chemistry ,Biochemistry ,Adrenal Medulla ,Organ Specificity ,Glutamic acid binding ,Neurology (clinical) ,Adrenal medulla ,Sodium acetate ,Developmental Biology - Abstract
A significant activity of L-[3H]glutamic acid binding was detected in the membranous particulate preparations obtained from the rat adrenal glands. In vitro addition of sodium acetate (100 mM) resulted in a drastic enhancement of the binding to cerebral preparations, while inducing a significant inhibition of the adrenal binding. Quisqualic acid elicited a prominent suppression of the adrenal binding in a concentration-dependent manner to a slightly greater extent than the inhibition of cerebral binding. N-Methyl-D-aspartic acid exerted a significant stimulatory action on the adrenal binding without affecting the cerebral binding. The adrenal medullary part possessed more than 5-fold higher binding activity than that in cortical part. These results suggest the possible existence of [3H]glutamate binding sites in rat adrenal glands which are distinctly different from those in the central structures.
- Published
- 1986
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