Chapter 1 Chairman's starting comments (pages 1–5): John C. Beck
Chapter 2 Biosynthesis of Insulin and Glucagon: A View of the present state-of-the-art (pages 7–30): Ake Lernmark, Shu Jin Chan, Rosa Choy, Anne Nathans, Raymond Carroll, Howard S. Tager, Arthur H. Rubenstein, Hewson H. rapid and Donald F. Steiner
Chapter three Molecular Evolution of the Polypetide Hormones (pages 31–59): Roger Acher
Chapter four Prohormones of ??Melanotropin (??Melanocyte?Stimulating Hormone, ??MSH) and Corticotropin (Adrenocorticotropic Hormone, ACTH): constitution and Activation (pages 61–75): A. F. Bradbury, D. G. Smyth and C. R. Snell
Chapter five the character of Pituitary huge progress Hormone as Studied through Immunoabsorption (pages 77–95): J. H. Livesey, D. Rubinsiein and J. C Beck
Chapter 6 Isolation of a Biologically lively Messenger RNA: guidance from Fish Pancreatic Islets via Oligo(2??Deoxythymidylic Acid) Affinity Chromatography (pages 97–116): M. Alan Permutt, Jan Biesbroeck, Rose Chyn, Irving Boime, Elzbieta Szczesna and Diana McWilliams
Chapter 7 The regulate of Insulin unlock by way of Sugars (pages 117–139): S. J. H. Ashcroft
Chapter eight The Mode of motion of Adenosine 3?:5??Cyclic Phosphate within the rules of Insulin Secretion (pages 141–158): W. Montague and S. L. Howell
Chapter nine a number of sorts of Corticotropin (Adrenocorticotropic Hormone, ACTH) and their value (pages 159–181): Rosalyn S. Yalow
Chapter 10 Carboxypeptidase B?Like and Trypsin?Like actions in remoted Rat Pancreatic Islets (pages 183–195): H. Zuuhlke, D. F. Steiner, A. Lernmark and C. Lipsey
Chapter eleven New thoughts within the Formation, law of unlock, and Metabolism of Parathyroid Hormone (pages 197–224): Joel F. Habener
Chapter 12 constitution and Structure?Function Relationships in Glycoprotein Hormones (pages 225–250): J. G. Pierce, M. R. religion, L. C. Giudice and J. R. Reeve
Chapter thirteen Heterogeneity of the Gastrins in Blood and Tissue (pages 251–265): R. A. Gregory
Chapter 14 Membrane Topology as printed by means of the Binding of Macromolecules (pages 267–280): L. Orci
Chapter 15 Protein Phosphorylation and Hormone motion (pages 281–295): Philip Cohen, John F. Antoniw, Hugh G. Nimmo and Stephen J. Yeaman
Chapter sixteen Growth?Promoting activities of Peptide Hormones (pages 297–369): J. R. Tata
Chapter 17 remaining feedback (pages 371–373): John C. Beck
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Additional resources for Ciba Foundation Symposium 41 - Polypeptide Hormones: Molecular and Cellular Aspects
J. Clin. Invest. 51, 912-921 RUBENSTEIN, A. , STARR, J. J. L. (1974) Circulating proinsulin in patients with islet cell tumors in Diabetes, Proceedings o f t h e Eighth Congress of the IDF (Malaise, W. J. ), pp. H. & GELLER, D. M. (1975) The structure of rat proalbumin. J. Biol. Chem. , TAKABATAKE, Y. & PORTANOVA, R. (1969) Biosynthesis and release of vasopressin and neurophysin. Rec. Frog. Horm. Res. 25, 447-484 I . , MCKEAN,D. , GUYER, R. & TERRY, W. ( I 975) Partial amino acid sequence SCHECHTER, of the precursor of immunoglobulin light chain programmed by messenger RNA in vitro.
CARPENTER, F. H. (1974) Carbonylbis(L-niethiony1)insulin. A proinstilin analog which is convertible to insulin. J. Am. Chem. Soc. A. & LAURIS,V. (1975) Beta cell culture o n synthetic capillaries: an artificial endocrine pancreas. Science (Wash. )187, 847-848 C HR ~ TI EN, M. & Lr, C. H. (1967) Isolation, purification and characterization of y-lipotropic hormone from sheep pituitary glands. Can. J. Biochem. S. -B. (1971) I n vitro stimulation of insulin release by non-metabolizable, transport-specific amino acids.
Furthermore, biosynthesis of the high molecular weight component and glucagon, as well as secretion of the hormone, are inhibited by high concentrations of glucose (Noe & Bauer 1971 ; Hellerstrom et al. 1972; O’Connor et al. 1973). Two peptides related to proglucagon have now been isolated. We reported the isolation from crystalline glucagon of a 37-residue peptide which contains the primary structure of the hormone at its NH,-terminus (Tager & Steiner 1973). The glucagon sequence is connected to the extension by the amino acid pair Lys-Arg.