Isolation and structure of hypothalamic MSH release-inhibiting hormone
| Autor: | R.M.G. Nair, Abba J. Kastin, Andrew V. Schally |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Electrophoresis
Proline Ultraviolet Rays MSH Release-Inhibiting Hormone Size-exclusion chromatography Glycine Hypothalamus Biophysics Peptide Biochemistry Fluorescence Mass Spectrometry chemistry.chemical_compound Isomerism Leucine Amide Animals Amino Acid Sequence Melanocyte-Stimulating Hormones Amino Acids Fragmentation (cell biology) Molecular Biology Peptide sequence Skin chemistry.chemical_classification Carbon Isotopes Neurotransmitter Agents Chromatography Edman degradation Cell Biology Amides chemistry Sephadex Depression Chemical Chromatography Gel Biological Assay Cattle Chromatography Thin Layer Anura Sulfonic Acids Peptides Pituitary Hormone-Releasing Hormones Thiocyanates |
| Zdroj: | Biochemical and Biophysical Research Communications. 43:1376-1381 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(71)80026-8 |
| Popis: | Summary MSH-release inhibiting hormone (MRIH) activity in bovine hypothalamic extracts, concentrated over 11,000-fold by gel filtration on Sephadex, was further purified by thin-layer chromatography. Two MRIH-active peptides were isolated; one showed a high and the other much weaker MRIH activity. The amino acid sequence of the main MRIH-active peptide, as determined by Edman degradation combined with the dansyl method, was shown to be prolyl-leucyl-glycine amide. These findings were confirmed by mass spectra. Synthetic L-Pro-L-Leu-glycine amide and the natural main MRIH-active peptide showed similar biological activities, chromatographic and electrophoretic mobilities, and mass spectral fragmentation patterns. This work indicates that the structure of bovine MRIH is L-Pro-L-Leu-Gly. NH 2 . |
| Databáze: | OpenAIRE |
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