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- W2045589600 abstract "alpha-MSH immunoreactive peptides were fractionated and characterized in rat and human brain and rat pituitary by reversed phase high pressure liquid chromatographic techniques. alpha-MSH and deacetylated alpha-MSH were two major naturally existing peptides in both brain and pituitary gland. Subsequent experiments examined the roles of these two peptides in neuronal function. The alpha-MSH was clearly more effective than deacetylated alpha-MSH in improving performance on a visual discrimination task after intraperitoneal administration and in inducing excessive grooming after intraventricular administration. The difference in behavioral potency may be explained by the fact that alpha-MSH was much more resistant to peptidase degradation than was deacetylated alpha-MSH. N-acetylation of alpha-MSH may be an effective regulatory process for modulating the behavioral potency of the secretory product of alpha-MSH-containing pituitary cells and neurons." @default.
- W2045589600 created "2016-06-24" @default.
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- W2045589600 date "1981-09-01" @default.
- W2045589600 modified "2023-10-14" @default.
- W2045589600 title "Evidence that N-acetylation regulates the behavioral activity of α-MSH in the rat and human central nervous system" @default.
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