Methods in Neurosciences: Neuropeptide Analogs, Conjugates and Fragments v. 13

Methods in Neurosciences: Neuropeptide Analogs, Conjugates and Fragments v. 13

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The volumes in this series include contemporary techniques significant to a particular branch of the neurosciences. They should be an invaluable aid to the student, as well as the experienced researcher, not only in developing protocols in the neurosciences, but in disciplines in which research is becoming closely related to the neurosciences. Convenient comb-bound editions are available for use by scientists at the bench. For the library, these volumes are available in quality casebound editions. Each volume of "Methods in Neurosciences" contains an index and each chapter includes references. Beginning with Volume 15, each volume will be assembled by a different editor. Dr Conn will remain as editor-in-chief of the series. This will further strengthen the depth of coverage in "Methods in Neurosciences" for students and researchers alike. This volume examines peptides. Peptides are informational molecules. The ability to manipulate their structure has made it possible to develop agonist and antagonist molecules, sometimes with remarkably greater activity than that found in the parent molecule.
Peptide analogs have been used for the development of quantitative assays and, by labelling them, have been helpful to tracer molecules. This volume is dedicated to the tricks and techniques for preparing and characterizing these molecules and to providing representative examples of their uses.
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Product details

  • Hardback | 384 pages
  • 203.2 x 230 x 25.4mm | 976g
  • Academic Press Inc
  • San Diego, United States
  • English
  • index
  • 012185275X
  • 9780121852757

Table of contents

Part 1 Synthesis and Characterization: F. Haviv and T.D. Fitzpatrick, Synthetic Approaches to Incorporation of Using Genadotropin-Releasing Hormone Animo Acids into Peptides. A.F. Spatola, Synthesis of Pseudopepfides. M. Chorev and M.P. Caulfield, Synthesis and Synthetic Manipulations of Peptides Derived from Parathoid Hormone and Parathoid Hormone-Related Protein. P.A. Anton, .F Shanaha, and J.P. Reeve Jr, Biotinylated Neuropeptide Analoges: Design and Use as Probes for Target Cells in Heterogeneous Populations. A.L. Smith, Using High-Performance Liquid Chromatography in Peptide Characterization and Purification. Part 2 Development and Use of Receptor Ligands: T. Inagami and Y. Kambayashi, Atrial Natriuritic Factors and Fragments. G.J. Trachte and B.J. Elmquist, Atrial Natriuritic Factors Binding to Clearance Receptors in Isolated Neuronal Membranes. E. Hazum and I. Schvartz, Biotinylated Endothelin Analogs as Probes for Endothelin Receptor. R. Miller, J.T. Pelton and C.R. Hiley, Analogs of Endothelin, C.W. Lin, T.A. Miller, B.B. Bianchi, and D.G. Witte, Selective Cholecystokinin A and Cholecystokinin-B/Gastrin Receptor Agonists. C.A. Maggi, Tachykinin Receptor Antagonists. K. Raynor and T. Reisine, Somatostatin Receptor Subtypes in Rat Brain Revealed by Somatostatin Analogs. N.A. Sharif, Thyrotropin-Releasing Hormone Analogs and Receptors. H. Shapiro, E. Wada, R. Jensen, and J. Battey, Distinguishing Bombesin Receptor Subtypes. J.P. Gies, A. Pifilieff, E.B. Haddad, and E. Lach, (Characterization Solubilization) Bombesin Receptor Subtypes. R.D. Smith, J.V. Duncia, P.J Lee, D.D. Christ, A.T. Chiu, D.J. Carini, W.F. Herblin, and P.B.M.W.M. Timmermans, R.R. Wexler, and P.C. Wong, Nonpeptide Angiotensin II Receptor Antagonist: Losartan. J. Howl and M. Wheatley, (Selective Biotinylated Probes) V1a Vasopressin Receptors: C. Barberis, T. Durroux, S. Audigier, M-N. Balestre, S. Jard, M. Manning, and W.H. Sawyer, V1a Vasopressin Receptors: Studies with a Radioiodinated Ligand. D. Butlen and A. Ammar, Pharmacological Identification of Vasopressin Receptors in Isolated Renal Tubule. Part 3 Development and Use of Antisera: R.W. Veh, H-W. Habbes, I.M. Grumbach, H.T. Pham, K-H. Meyer and J. Czekalla, Neuropeptide Conjugation to Carrier Proteins. M. Mori, T. Satoh, and M. Yamada, Anti-Idiotypic Thyrotropin-Releasing Hormone (TRH) Antibody. K. Rissler, H. Cramer, and G. Friedrich, (Influence of Oxidation State) 125I-Labelled Substance P on Sensitivity of Radioimmunoassay.
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