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Isolation of a brain peptide identical to the intestinal PHI (peptide HI) |
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| Authors: | K Tatemoto M Carlquist T J McDonald V Mutt |
| Institution: | Laboratoire de Photosynthèse, CNRS, BP 1, 91190 Gif sur Yvette, France |
| Abstract: | The isolation of a brain peptide identical to the intestinal peptide PHI (peptide HI) is described. The peptide was isolated from porcine brain extract using a chemical assay method based on its C-terminal isoleucine amide structure. The complete amino acid sequence of the peptide was found to be: His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Phe-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser-Ala- Lys-Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2. This sequence is identical to the intestinal peptide thus demonstrating PHI to be a brain-gut peptide. The role of PHI in the central nervous system as a neurotransmitter or neuromodulator is discussed. |
| Keywords: | Electron transfer Proton gradient Phosphorylation Membrane topography Microchemiosmosis Thylakoid ΔpH ΔΨ transmembrane differences of the proton electrochemical potential of pH and of electric potential respectively a top bar indicates mean as experimentally measured values the local situation at the coupling factor level SI SII (photo)systems I II CF coupling factor plastoquinone plastoquinol DBMIB dibromothymoquinone |
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