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R Burgus

Publications and source records attributed to R Burgus.

At least 19 recordsLinked to original sources
PubMed1976

[Endorphins, hypothalamic and neurohypophysial peptides with morphinomimetic activity: isolation and molecular structure of alpha-endorphin].

From a crude extract of Porcine neurohypophysis-hypothalamus we have isolated several peptides called endorphins which mimic opiated in a classical bioassay for morphine. Similarly they bind to the stereospecific synaptosomal opiates receptors of Rat brain in competition to 3 H-etorphine. The primary structure of alpha-endorphin is H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH. Met-enkephalin is the N-terminal pentapeptide of alpha-endorphin. Alpha-endorphin has the same sequence as that of the fragment TYR 61 to Thr 76 of the beta-lipotropins.

Amino Acid Sequence↗
PubMed1976

Isolation, primary structure, and synthesis of alpha-endorphin and gamma-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity.

The isolation and primary structure of two peptides with morphinomimetic activity, obtained from an extract of porcine hypothalamus-neurohypophysis, are described. The amino acid sequence of the two peptides, named alpha-endorphin and gamma-endophin, was determined by mass spectrometry and danxyl-Edman methods to be H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH and H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-OH, respectively. These correspond to the amino acid sequences present between residues 61 and 76 and residues 61 and 77 of the various beta-lipotropins. A third peptide also obtained in pure form in these studies was found to be an unstable salt of alpha-endorphin.

Amino Acid Sequence↗
PubMed1975

Somatostatin.

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Amino Acid Sequence↗
PubMed1973

Primary structure of somatostatin, a hypothalamic peptide that inhibits the secretion of pituitary growth hormone.

Somatostatin, a peptide isolated from ovine hypothalamic tissue that inhibits the release of radioimmunoassayable growth hormone in vitro from rat or human pituitary cells or in vivo in rats, has the primary structure [Formula: see text]. The structure was established by submitting the carboxymethylated peptide, the carboxymethylated tryptic digest, and the chymotryptic digest of the peptide to Edman degradation. Degradation products were analyzed by amino-acid analysis, as well as in some cases by determination of N-termini by dansylation or by determination of phenylthiohydantoins by mass spectrometry.

Amino Acid Sequence↗