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1. Control of Anterior Pituitary Hormone Secretion

Author

R. Burgus, C Gilon, G. Grant, C. Rivier, M. Monahan, Vale W, N Ling, M. Amoss, P. Brazeau, Guillemin R, and Rivier J

Subjects
medicine.medical_specialty, Basophil cell, Somatotropic cell, Neuroendocrinology, Biology, Gonadotropic cell, Endocrinology, medicine.anatomical_structure, Anterior pituitary, Thyrotropic cell, Internal medicine, medicine, Secretion, Corticotropic cell
Published
2015
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2. Lack of effect of native or synthetic LRF on secretion of prolactin in vitro

Author

N Ling, Guillemin R, Vale W, R. Burgus, R. Blackwell, M. Amoss, Rivier J, and M. Monahan

Subjects
Male, medicine.medical_specialty, Sheep, Immune Sera, Radioimmunoassay, In Vitro Techniques, Biology, In vitro, Prolactin, Rats, Endocrinology, Pituitary Gland, Physiology (medical), Internal medicine, medicine, Animals, Female, Secretion, Pituitary Hormone-Releasing Hormones, Cells, Cultured
Published
1973
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3. Concomitant release of FSH and LH induced by native and synthetic LRF

Author

Rivier J, R. Blackwell, N Ling, M. Amoss, M. Monahan, R. Burgus, Vale W, and Guillemin R

Subjects
medicine.medical_specialty, Sheep, Chemistry, business.industry, Immune Sera, Radioimmunoassay, In Vitro Techniques, Luteinizing Hormone, Stimulation, Chemical, Rats, Endocrinology, Text mining, Pituitary Gland, Physiology (medical), Concomitant, Internal medicine, medicine, Animals, Follicle Stimulating Hormone, business, Pituitary Hormone-Releasing Hormones
Published
1973
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4. In vitro Plasma Inactivation of Thyrotropin Releasing Factor (TRF) and Related Peptides. Its Inhibition by Various Means and by the Synthetic Dipeptide PCA-His-OME

Author

R. Burgus, Dunn Tf, R. Guillemin, and Wylie Vale

Subjects
chemistry.chemical_classification, Dipeptide, Endocrinology, Diabetes and Metabolism, Biological activity, In Vitro Techniques, Rat blood, Molecular biology, In vitro, Rats, Plasma, chemistry.chemical_compound, Thyrotropin-releasing factor, Endocrinology, Enzyme, chemistry, Biochemistry, Pediatrics, Perinatology and Child Health, Animals, Thyrotropin-Releasing Hormone, Incubation
Abstract

Incubation in vitro of natural (ovine) or synthetic TRF (PCA-His-Pro-NH2) with rat blood, plasma, or reconstituted lyophilized serum destroys the biological activity. Inactivation of TRF by normal plasma takes place at 0 °C but at a slower rate than at 37 °C. Plasma obtained from rats several weeks after hypophysectomy and/ or hypophysectomy + thyroidectomy inactivates TRF. TRF activity is not recovered from TRF incubated in plasma when the incubate is treated with NaCl (4 m), ethanol (80% v/v) or HCl (to pH 1). Plasma inactivation of TRF is completely prevented by pretreatment of the plasma with ethanol (80% v/v); heating of plasma at 65 °C for 15 min also destroys the ability of plasma to inactivate TRF. The data reported are consistent with the hypothesis that plasma contains an enzyme (s) which destroys the activity of TRF. Plasma was also found to destroy the biological activity of PCA-His-Pro-OMe and PCA-His-Pro-OH (2 synthetic tripeptides with TRF activity). The biological activity of PCA-His-Pro-OH is destroyed in vitro at a slower rate by plasma than that of PCA-His-Pro-NH2 or natural TRF. Addition of the dipeptide analogue of TRF, PCA-His-OMe, prevents in vitro the inactivation of TRF by plasma.

Published
1971
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5. Contents, Vol. 2, 1971/72

Author

G. Chieffi, D.H. Pemberton, J. Rivier, I.A. Cumming, Josephine Milner, K.B. Eik-Nes, M. Amoss, Marion Jackson, W.H. Rotsztejn, W.I.P. Mainwaring, S. Heller, Ghislaine Gallez, Christine Waelbroeck, J. Ghirlanda, G. Copinschi, R. Blackwell, G. Verhoeven, C. Kordon, R.S. Mical, S. Badawy, A.S. Goldman, R. Guillemin, J.-C. Heuson, A. Guitelman, R. Burgus, R. Johansson, L. Iela, M. Rajalakshmi, F.R. Mangan, W.A. Chamley, H.D. Schlumberger, R.E. Mancini, J.M. Brown, A. van den Ende, F. Neumann, J.C. Cerini, R.K. Rastogi, J.K. Findlay, A. Gillespie, F. Gogan, O.M. Cramer, G. Materazzi, R. Massa, H. Hassouna, P.R.K. Reddy, P. de Moor, rez Lloret, Denise E. Bu, Nicole Legros, C.C. Chang, M. Hery, K. Loewit, M. Monahan, Aliza Eshkol, Mildred E.D. Cerini, C. Robyn, R.S. Santti, J.R. Goding, M.D. Cain, L. Martini, W. Vale, K.A. Laurence, M.R.N. Prasad, R.G.A. van Wayjen, B. Scattolini, J.C. Porter, G. Grant, A. Jost, J.L. Pasteels, Shea, N. Ling, B. Lunenfeld, and Lupo di Prisco

Subjects
Reproductive Medicine, Obstetrics and Gynecology
Published
1971
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6. LIST OF CONTRIBUTORS AND DISCUSSANTS

Author

J.A. Archer, A. Arimura, G.D. Aurbach, J. Axelrod, R.S. Bar, A. Bartke, D.B. Bartosik, F.C. Bartter, M. Beato, J.C. Beck, N.H. Bell, V. Bennett, L. Birnbaumer, E.M. Bogdanove, B. Boss, R.M. Boyar, E.D. Bransome, P. Brazeau, H.J. Brodie, J.C. Brown, M. Brown, R. Burgus, G.N. Burrow, G.T. Campbell, S. Cataland, Kwen-Jen Chang, L.R. Chase, S.L. Cohen, P. Colman, P.G. Condliffe, B.A. Cross, P. Cuatrecasas, I.J. Davies, P. De Meyts, B.M. Dobyns, M.B. Dratman, M. Drosdonsky, J.R. Dryburgh, J. Dupré, R.E.J. Dyball, R.G. Dyer, P. Feigelson, F. Flores, P. Freychet, H.G. Friesen, J.W. Funder, J.R. Gavin, V.L. Gay, J.M. George, J.R. Gill, S. Glick, I.D. Goldfine, H.M. Goodman, P. Gorden, R.O. Creep, M.A. Greer, R. Guillemin, S.L. Gupta, A. Haksar, S.N.S. Hanjan, G.A. Hedge, L. Hellman, M. Herman, J.M. Hershman, M.D. Hollenberg, R. Jewelewicz, C.W. Jones, C.R. Kahn, M. Kalimi, S. Kapen, F.J. Karsch, A.D. Kenny, L.A. Killewich, J.I. Kitay, E. Knobil, J. Konishi, J. Kowal, D.T. Krieger, R. Krishnaraj, J.P. Kriss, M. Kuhn, N. Kumar, B.L. Lasley, H. Leblanc, R.M. Lequin, M.A. Lesniak, R. Levy, D.W. Lincoln, N. Ling, M.B. Lipsett, S.M. McCann, J.M. McKenzie, G.S. McKnight, W.B. Malarky, B.H. Marks, K. Megyesi, J.C. Melby, C. Monder, J.F. Morris, F. Naftolin, D.M. Neville, M.B. Nikitovitch-Winer, S.J. Nillius, J.M. Nolin, R. Palacios, M.R. Pandian, J.A. Parsons, Z. Petro, B.T. Pickering, B.I. Posner, S. Raiti, J.A. Ramaley, V.V. Reddy, B.F. Rice, C. Rivier, J. Rivier, J.S. Roberts, R. Rolland, A.L. Rosenbloom, S.A. Ross, J. Roth, K.J. Ryan, N. Samaan, R.J. Santen, R.K. Saxena, R.T. Schimke, E. Schonbaum, G. Schutz, N.B. Schwartz, A.A. Shaikh, D.J. Shapiro, R.J. Sherins, T.M. Siler, H.W. Sokol, A.H. Soil, K. Sterling, D. Sulhvan, D. Sunde, Y. Takaoka, G.P. Talwar, T.C. Theoharides, J.L. Vaitukaitis, W. Vale, H. Valtin, W.P. Vander Laan, C.A. Villee, C.F. Wang, R.F. Weick, J. Weisz, E.D. Weitzman, A. White, R.J. White, L. Wolin, and S.S.C. Yen

Published
1975
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7. Somatostatin

Author

W, Vale, P, Brazeau, C, Rivier, M, Brown, B, Boss, J, Rivier, R, Burgus, N, Ling, and R, Guillemin

Subjects
Brain, Thyrotropin, Estrogens, Luteinizing Hormone, Prolactin, Rats, Islets of Langerhans, Structure-Activity Relationship, Organ Specificity, Pituitary Gland, Anterior, Growth Hormone, Animals, Triiodothyronine, Amino Acid Sequence, Cycloheximide, Somatostatin, Cells, Cultured, Progesterone
Published
1975

9. Isolation of somatostatin (a somatotropin release inhibiting factor) of ovine hypothalamic origin

Author

R. Guillemin, P. Brazeau, R. Burgus, and W. Vale

Subjects
medicine.medical_specialty, Optical Rotation, Hypothalamus, Radioimmunoassay, Ultrafiltration, Nerve Tissue Proteins, Growth Hormone-Releasing Hormone, Internal medicine, medicine, Animals, Electrophoresis, Paper, Amino Acids, Countercurrent Distribution, Somatotropin secretion, Sheep, Chemistry, General Medicine, Chromatography, Ion Exchange, Molecular Weight, Endocrinology, Somatostatin, Growth Hormone, Chromatography, Gel, Biological Assay, Electrophoresis, Polyacrylamide Gel, Spectrophotometry, Ultraviolet, Chromatography, Thin Layer
Abstract

Isolation of somatostatin, a tetradecapeptide of ovine origin inhibiting somatotropin secretion, is reported. About 490 000 hypothalamic fragments were submitted to alcohol–chloroform extraction, countercurrent distribution, ion-exchange chromatography, gel filtration, and partition chromatography. Of the 8.5 mg material thus obtained, 77% was accounted for by a peptide shown homogeneous by electrophoresis, thin-layer chromatography, and amino acid analysis. The peptide inhibits the secretion of radioimmunoassayable growth hormone at doses of ≥ 1.0 nM in vitro and 400 ng per rate in vivo.

Published
1974

10. Isolation and characterization of hypothalamic peptide hormones

Author

R, Burgus, M, Amoss, P, Brazeau, M, Brown, N, Ling, C, Rivier, J, Rivier, W, Vale, and J, Villarreal

Subjects
Brain Chemistry, Gonadotropin-Releasing Hormone, Pituitary Hormone Release Inhibiting Hormones, Hypothalamus, Animals, Biological Assay, Growth Hormone-Releasing Hormone, Prolactin Release-Inhibiting Factors, Somatostatin, Pituitary Hormone-Releasing Hormones, Thyrotropin-Releasing Hormone, MSH Release-Inhibiting Hormone, Myelin Proteins
Published
1976

12. [Synthetic polypeptide derivatives with TRF hypophysiotropic activity. New data]

Author

R, Burgus, T F, Dunn, D, Desiderio, W, Vale, and R, Guillemin

Subjects
Chemical Phenomena, Proline, Infrared Rays, Methanol, Spectrum Analysis, Acetates, Chromatography, Ion Exchange, Anhydrides, Chemistry, Glutamates, Pituitary Gland, Chromatography, Gel, Histidine, Hydrochloric Acid, Peptides, Thyrotropin-Releasing Hormone
Published
1969

13. Solubility of the hypothalamic hormones TSH-releasing factor (TRF) and LH-releasing factor (LRF) in organic and alcoholic solvents

Author

R. Burgus, R. Guillemin, and Max S. Amoss

Subjects
Pharmacology, Stereochemistry, Chemistry, Pyridines, Methanol, Thyrotropin-releasing hormone, Cell Biology, Luteinizing Hormone, Molecular biology, Cellular and Molecular Neuroscience, Hypothalamic Hormones, Solubility, TSH-releasing factor, Solvents, Molecular Medicine, Chloroform, Molecular Biology, Pituitary Hormone-Releasing Hormones, Thyrotropin-Releasing Hormone
Abstract

L'hormone hypothalamique TRF (TSH-releasing factor) est soluble dans l'alcool methylique a 90%, partiellement soluble dans l'alcool methylique absolu ou le chloroforme; TRF n'est pas soluble dans la pyridine. Le chlorure de methylene (dichloromethane) n'extrait pas le TRF d'une solution aqueuse (preparation hautement purifiee, 15000 U/mg). L'hormone hypothalamique LRF (LH-releasing factor) n'est pas soluble dans le chloroforme mais est soluble dans l'alcool methylique absolu ou a 90%.

Published
1967

18. The hypothalamic hypophysiotropic thyrotropin-releasing factor

Author

R, Guillemin, R, Burgus, and W, Vale

Subjects
Hypothalamo-Hypophyseal System, Sheep, Protein Conformation, Swine, Mass Spectrometry, Rats, Mice, Structure-Activity Relationship, Iodine Isotopes, Chromatography, Gel, Animals, Humans, Cattle, Amino Acid Sequence, Amino Acids, Thyrotropin-Releasing Hormone
Published
1971

19. Chemistry of hypothalamic releasing factors

Author

R, Burgus, W, Vale, J, Rivier, M, Monahan, N, Ling, G, Grant, M, Amoss, and R, Guillemin

Subjects
Gonadotropin-Releasing Hormone, Chemistry, Structure-Activity Relationship, Chemical Phenomena, Hypothalamus, Thyrotropin-Releasing Hormone
Published
1973

20. [Preliminary observations on the mechanism of action of somatostatin, a hypothalamic factor inhibiting the secretion of growth hormone]

Author

W, Vale, P, Brazeau, G, Grant, A, Nussey, R, Burgus, J, Rivier, N, Ling, and R, Guillemin

Subjects
Carbon Isotopes, Hypothalamus, Radioimmunoassay, Tritium, Rats, Butyrates, Theophylline, Leucine, Culture Techniques, Growth Hormone, Cyclic AMP, Animals, Electrophoresis, Polyacrylamide Gel, Pituitary Hormone-Releasing Hormones, Cells, Cultured
Published
1972

29. Presence of calcium ions as a requisite for the in vitro stimulation of TSH-release by hypothalamic TRF

Author

R. Guillemin, W. Vale, and R. Burgus

Subjects
Male, endocrine system, medicine.medical_specialty, Hypothalamo-Hypophyseal System, endocrine system diseases, Hypothalamus, chemistry.chemical_element, Thyrotropin, Calcium, In vitro stimulation, Cellular and Molecular Neuroscience, Internal medicine, Culture Techniques, medicine, Animals, Molecular Biology, Thyrotropin-Releasing Hormone, Pharmacology, Cell Biology, Culture Media, Rats, Endocrinology, chemistry, Pituitary Gland, Molecular Medicine, hormones, hormone substitutes, and hormone antagonists
Abstract

L'incubation in vitro de fragments d'hypophyse (rat) dans le liquide de Krebs-Ringer sans calcium (Ca++) inhibe l'action du facteur hypothalamique TRF (TSH-releasing factor) qui normalement stimule la secretion de l'hormone thyreotrope (TSH). La re-introduction de l'ion Ca++ (2.54 mM) retablit la reponse (secretion de TSH) au facteur TRF.

Published
1967

30. Isolation of somatostatin (a somatotropin release inhibiting factor) of ovine hypothalamic origin.

Author

Brazeau P, Vale W, Burgus R, and Guillemin R

Subjects
Amino Acids analysis, Animals, Biological Assay, Chromatography, Gel, Chromatography, Ion Exchange, Chromatography, Thin Layer, Countercurrent Distribution, Electrophoresis, Paper, Electrophoresis, Polyacrylamide Gel, Growth Hormone metabolism, Molecular Weight, Nerve Tissue Proteins analysis, Optical Rotation, Radioimmunoassay, Sheep, Spectrophotometry, Ultraviolet, Ultrafiltration, Growth Hormone-Releasing Hormone antagonists & inhibitors, Hypothalamus analysis, Nerve Tissue Proteins isolation & purification
Published
1974
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31. The endorphins, novel peptides of brain and hypophysial origin, with opiate-like activity: biochemical and biologic studies.

Author

Guillemin R, Ling N, Lazarus L, Burgus R, Minick S, Bloom F, Nicoll R, Siggins G, and Segal D

Subjects
Animals, Brain Chemistry, Cattle, Dose-Response Relationship, Drug, Endorphins isolation & purification, Immunochemistry, Pituitary Hormones metabolism, Rats, Sheep, Swine, beta-Lipotropin pharmacology, Behavior, Animal drug effects, Brain drug effects, Endorphins pharmacology
Published
1977
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32. Characterization of the endorphins, novel hypothalamic and neurohypophysial peptides with opiate-like activity: evidence that they induce profound behavioral changes.

Author

Guillemin R, Ling N, Burgus R, Bloom F, and Segal D

Subjects
Animals, Biological Assay, Enkephalins analysis, Enkephalins pharmacology, Hypothalamus analysis, Injections, Intraventricular, Myenteric Plexus drug effects, Pituitary Gland, Posterior analysis, Rats, Behavior, Animal drug effects, Endorphins pharmacology
Published
1977
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33. Myelin basic protein: a substance that releases immunoreactive growth hormone in vitro.

Author

Villarreal JA, Vale W, Brown M, Butcher M, Brazeau P, Rivier C, and Burgus R

Subjects
Amino Acids analysis, Animals, Cattle, Macromolecular Substances, Myelin Basic Protein isolation & purification, Pituitary Gland drug effects, Pituitary Gland metabolism, Prostaglandins E pharmacology, Sheep, Species Specificity, Growth Hormone-Releasing Hormone, Hypothalamus physiology, Myelin Basic Protein physiology
Published
1976
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34. [Endorphins, hypothalamic and neurohypophysial peptides with morphinomimetic activity: isolation and molecular structure of alpha-endorphin].

Author

Guillemin R, Ling N, and Burgus R

Subjects
Amino Acid Sequence, Animals, Biological Assay, Cattle, Morphine metabolism, Nerve Tissue Proteins isolation & purification, Peptides chemical synthesis, Peptides isolation & purification, Rats, Receptors, Drug, Swine, Hypothalamus analysis, Nerve Tissue Proteins analysis, Peptides analysis, Pituitary Gland, Posterior analysis
Abstract

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.

Published
1976

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

Author

Ling N, Burgus R, and Guillemin R

Subjects
Amino Acid Sequence, Animals, Peptides analysis, Peptides chemical synthesis, Swine, Hypothalamus chemistry, Nerve Tissue Proteins analysis, Nerve Tissue Proteins chemical synthesis, Pituitary Gland, Posterior chemistry
Abstract

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.

Published
1976
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37. Isolation and characterization of hypothalamic peptide hormones.

Author

Burgus R, Amoss M, Brazeau P, Brown M, Ling N, Rivier C, Rivier J, Vale W, and Villarreal J

Subjects
Animals, Biological Assay, Brain Chemistry, Gonadotropin-Releasing Hormone analysis, Gonadotropin-Releasing Hormone isolation & purification, Growth Hormone-Releasing Hormone isolation & purification, MSH Release-Inhibiting Hormone isolation & purification, Myelin Proteins isolation & purification, Prolactin Release-Inhibiting Factors isolation & purification, Somatostatin isolation & purification, Thyrotropin-Releasing Hormone isolation & purification, Hypothalamus analysis, Pituitary Hormone Release Inhibiting Hormones isolation & purification, Pituitary Hormone-Releasing Hormones isolation & purification
Published
1976
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38. Somatostatin.

Author

Vale W, Brazeau P, Rivier C, Brown M, Boss B, Rivier J, Burgus R, Ling N, and Guillemin R

Subjects
Amino Acid Sequence, Animals, Brain physiology, Cells, Cultured, Cycloheximide pharmacology, Estrogens pharmacology, Growth Hormone metabolism, Islets of Langerhans drug effects, Islets of Langerhans metabolism, Luteinizing Hormone metabolism, Organ Specificity, Pituitary Gland, Anterior drug effects, Pituitary Gland, Anterior metabolism, Progesterone pharmacology, Prolactin metabolism, Rats, Structure-Activity Relationship, Thyrotropin metabolism, Triiodothyronine pharmacology, Somatostatin isolation & purification, Somatostatin pharmacology, Somatostatin physiology
Published
1975
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39. Synthetic polypeptide antagonists of the hypothalamic luteinizing hormone releasing factor.

Author

Vale W, Grant G, Rivier J, Monahan M, Amoss M, Blackwell R, Burgus R, and Guillemin R

Subjects
Animals, Cells, Cultured, Pituitary Gland cytology, Pituitary Gland metabolism, Rats, Receptors, Drug, Structure-Activity Relationship, Luteinizing Hormone metabolism, Peptides pharmacology, Pituitary Hormone-Releasing Hormones antagonists & inhibitors
Abstract

Two analogs of the hypothalamic luteinizing hormone releasing factor modified at the histidine-2 position were tested for biological activity (secretion of luteinizing hormone) in cultures of dispersed rat anterior pituitary cells. The analog in which glycine was substituted for histidine at position 2, [Gly(2)]LRF, behaves as a partial agonist releasing less than 50 percent of the luteinizing hormone secreted at maximum concentrations of the releasing factor, while the analog in which histidine at position 2 is deleted has no significant agonist activity at any of the doses tested. When added to the cultured cells at molar ratios 10(3) to 10(4) times that of the luteinizing hormone releasing factor, both analogs decrease the amount of luteinizing hormone secreted in response to the releasing factor.

Published
1972
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40. Primary structure of the ovine hypothalamic luteinizing hormone-releasing factor (LRF) (LH-hypothalamus-LRF-gas chromatography-mass spectrometry-decapeptide-Edman degradation).

Author

Burgus R, Butcher M, Amoss M, Ling N, Monahan M, Rivier J, Fellows R, Blackwell R, Vale W, and Guillemin R

Subjects
Amino Acid Sequence, Amino Acids analysis, Animals, Carbon Isotopes, Carboxypeptidases, Chromatography, Gas, Chromatography, Thin Layer, Chymotrypsin, Dansyl Compounds, Hydrolysis, Mass Spectrometry, Peptide Chain Termination, Translational, Peptides analysis, Sheep, Hypothalamus analysis, Luteinizing Hormone analysis, Pituitary Hormone-Releasing Hormones analysis
Abstract

The primary structure of ovine hypothalamic hypophysiotropic luteinizing hormone-releasing factor, LRF, has been established as pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH(2) by hydrolysis of the peptide with chymotrypsin or pyrrolidone-carboxylylpeptidase and by analysis of the products by an Edman-dansylation sequencing technique, as well as by mass spectrometry of the derived phenylthiohydantoins. A decapeptide with the proposed primary structure, prepared by total synthesis, gave the same result on sequencing. The synthetic decapeptide possesses the same biological activities as the native ovine LRF. The amino-acid sequence of ovine LRF is identical to that already published for porcine LRF.

Published
1972
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41. Polypeptides antagonists of the hypothalamic luteinizing hormone releasing factor.

Author

Guillemin R, Amoss M, Blackwell R, Burgus R, Grant G, Ling N, Monahan M, Rivier J, and Vale W

Subjects
Amino Acid Sequence, Animals, Cells, Cultured, Glycine, Histidine, Hypothalamus, Male, Pituitary Gland metabolism, Rats, Luteinizing Hormone metabolism, Peptides pharmacology, Pituitary Hormone-Releasing Hormones antagonists & inhibitors
Published
1971

42. Synthetic thyrotropin-releasing factor analogs. 3. Effect of replacement or modification of histidine residue on biological activity.

Author

Rivier J, Vale W, Monahan M, Ling N, and Burgus R

Subjects
Amino Acids chemical synthesis, Animals, Chromatography, Thin Layer, Infrared Rays, Magnetic Resonance Spectroscopy, Mass Spectrometry, Mice, Peptides chemical synthesis, Protein Conformation, Spectrum Analysis, Structure-Activity Relationship, Histidine chemical synthesis, Thyrotropin-Releasing Hormone chemical synthesis
Published
1972
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45. Synthetic luteinizing hormone-releasing factor analogs. Series of short-chain amide LRF homologs converging to the amino terminus.

Author

Rivier J, Vale W, Burgus R, Ling N, Amoss M, Blackwell R, and Guillemin R

Subjects
Amides chemical synthesis, Amino Acid Sequence, Amino Acids analysis, Animals, Chromatography, Ion Exchange, Chromatography, Thin Layer, Follicle Stimulating Hormone metabolism, Peptide Chain Termination, Translational, Pituitary Gland drug effects, Pituitary Hormone-Releasing Hormones pharmacology, Luteinizing Hormone metabolism, Pituitary Hormone-Releasing Hormones chemical synthesis
Published
1973
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48. Variability of response in the bioassay for a hypothalamic somatotrophin releasing factor based on rat pituitary growth hormone content.

Author

Rodger NW, Beck JC, Burgus R, and Guillemin R

Subjects
Animals, Chromatography, Gel, Female, Growth Hormone analysis, Hypophysectomy, Pituitary Gland analysis, Radioimmunoassay, Rats, Sheep, Swine, Tibia drug effects, Tissue Extracts, Biological Assay, Growth Hormone metabolism, Hypothalamo-Hypophyseal System physiology, Hypothalamus analysis, Pituitary Hormone-Releasing Hormones analysis
Published
1969
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49. Primary structure of somatostatin, a hypothalamic peptide that inhibits the secretion of pituitary growth hormone.

Author

Burgus R, Ling N, Butcher M, and Guillemin R

Subjects
Amino Acid Sequence, Animals, Autoanalysis, Chemical Precipitation, Chymotrypsin, Growth Hormone antagonists & inhibitors, Mass Spectrometry, Pituitary Gland drug effects, Pituitary Gland metabolism, Sheep, Trypsin, Growth Hormone metabolism, Hypothalamus, Peptides pharmacology, Tissue Extracts pharmacology
Abstract

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.

Published
1973
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