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Galanin — a novel biologically active peptide from porcine intestine

FEBS Letters · 1983 · Vol. 164(1) · pp. 124–128
Kazuhiko TatemotoÅke RökaeusHans JörnvallThomas J. McDonaldViktor Mutt

Abstract

The isolation of a novel biologically active peptide, designated galanin, is described. The peptide was discovered by the detection of its C-terminal amide structure in porcine intestinal extract using a chemical method. It was found that galanin consists of 29 amino acids and the complete amino acid sequence is: Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-Leu-Leu-Gly-Pro-His-Ala-Ile-Asp-Asn-His -Arg-Ser -Phe-His-Asp-Lys-Tyr-Gly-Leu-Ala-NH2. Galanin was found to contract smooth muscle preparations from the rat and to cause a mild and sustained hyperglycemia in dog.

Neuropeptides and Animal PhysiologyPeptidase Inhibition and AnalysisReceptor Mechanisms and SignalingGalaninPeptideAmino acidChemistryNeuropeptideBiological activityBiochemistryPeptide sequenceIn vitroReceptor

MeSH terms

Amino Acid SequenceAmino AcidsAnimalsBiological AssayBlood GlucoseIntestine, SmallMuscle ContractionPeptidesSwineGalaninRats
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References
Structure of the porcine LH- and FSH-releasing hormone. I. The proposed amino acid sequence
Biochemical and Biophysical Research Communications · 1971 · 1,126 citations
Structure of the porcine LH- and FSH-releasing hormone. I. The proposed amino acid sequence
American Journal of Obstetrics and Gynecology · 1976 · 1,032 citations
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Galanin — a novel biologically active peptide from porcine intestine · Scinovex