Hormone Action, Part K: Neuroendocrine Peptides

Volume 168: Hormone Action Part K

Sorozatcím: Methods in Enzymology; 168;

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A termék adatai:

Kiadó Elsevier Science
Megjelenés dátuma 1989. május 1.

ISBN 9780121820695
Kötéstípus Keménykötés
Terjedelem906 oldal
Méret 229x152 mm
Súly 1650 g
Nyelv angol

Kategóriák

Sejttan Biokémia Fiziológia, élettan, anyagcsere Endokrinológia, diabetológia Biofizika

Hosszú leírás:

Volume 168 of Methods in Enzymology will prove invaluable not only to those in the field but also to those in related disciplines who find their studies becoming closely linked to the neurosciences. Methodologies are presented to allow easy adaptation to new systems and to stress their general applicability and potential limitations.

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Tartalomjegyzék:

Preparation of Chemical Probes:
M.C. Beinfeld, Strategy and Methodology for the Development of Antisera against Procholecystokinin.
J.P. Tam, A High-Density Multiple Antigen Peptide System for the Preparation of Antipeptide Antibodies.
K.L. Bost and J.E. Blalock, Preparation and Use of Complementary Peptides.
J. Schwartz and W. Vale, Fluorescent and Cytotoxic Analogs of CRF Probes for Studying Target Cells in Heterogeneous Populations.
Equipment and Technology:
C. Denef, Methods to Study Cell-to-Cell Communication in Peptide Target Cells of the Anterior Pituitary.
P.C. Andrews and J.E. Dixon, Application of Fast Atom Bombardment Mass Spectrometry to Posttranslational Modifications of Neuropeptides.
E.D. French and J.T. Williams, Electrophysiological Analysis of Opioid Peptides: Extracellular and Intracellular Approaches.
M.I. Phillips and R.A. Palovcik, Dose Response Testing of Peptides by Hippocampal Brain Slice Recording.
T.L. Croxton, W.McD. Armstrong, and N. Ben-Jonathan, Patch Clamp Recording from Anterior Pituitary Cells Identified by a Reverse Hemolytic Plaque Assay.
J.E. Levine and K.D. Powell, Microdialysis for Measurement of Neuroendocrine Peptides.
K.M. Kendrick, Use of Microdialysis in Neuroendocrinology.
D.D. Rasmussen, In Vitro Perifusion of Human Hypothalamic and Pituitary Tissue.
I. Winicov and M.C. Gershengorn, Transient Permeabilization of Endocrine Cells: A New Approach to the Study of Inositol Lipid Metabolism.
T.F.J. Martin, Cell-Cracking: Permeabilizing Cells to Macromolecular Probes.
I. Murai, W.C. Low, and N. Ben-Jonathan, Microsurgical Techniques for Studying Functional Correlates of Hypothalamohypophysal Axis.
G. Martinez de la Escalera, K.C. Swearingen, and R.I. Weiner, Superfusion and Static Culture Techniques for Measurement of Rapid Changes in Prolactin Secretion.
D.A. Leong, Direct Observation of Intracellular Calcium Levels in Single Rat Anterior Pituitary Cells.
Preparation and Maintenance of Biological Materials:
C.A. McArdle and P.M. Conn, The Use of Protein Kinase C-Depleted Cells for Investigation of the Role of Protein Kinase C in Stimulus-Response Coupling in the Pituitary.
J. Eng and R.S. Yalow, Purification of Neuropeptides: CCK8 and VIP.
C.D. Scott and R.C. Baxter, Purification and Characterization of Insulinlike Growth Factor II Receptors.
Quantitation of Neuroendocrine Substances:
M.E. Kendall and W.C. Hymer, Measurement of Hormone Secretion from Individual Cells by the Cell Blot Assay.
M.M. Chien and J.C. Cambier, Measurement of Receptor Coupling to Phosphoinositide Hydrolysis across Isolated Cell Membranes.
M.S. Shearman, K. Ogita, U. Kikkawa and Y. Nishizuka, Rapid Method for the Resolution of Protein Kinase C Subspecies from Rat Brain Tissue.
T. Brock, J. Humm, and J.S. Kizer, Assay of Peptidylglycine Monooxygenase: Glycine-Directed Amidating Enzyme.
J.B. Koger, J. Humm, and J.S. Kizer, Assay of Glutaminylpeptide Cyclase.
C.H. Emerson, Primary Thyrotropin-Releasing Hormone-Degrading Enzymes.
J.C. Porter, P.S. Wang, W. Kedzierski, and H.A. Gonzalez, Quantification of the Mass of Tyrosine Monooxygenase in the Median Eminence and Superior Cervical Ganglion.
J.P.H. Burbach and B. Liu, Measurement of Vasopressin-Converting Aminopeptidase Activity and Vasopressin Metabolites.
H.H.M. Van Tol and J.P.H. Burbach, Quantitation of Vasopressin and Oxytocin mRNA Levels in the Brain.
K.D. Dahn, X.-C. Jia, and A.J.W. Hsueh, Granulosa Cell Aromatase Bioassay for Follicle-Stimulating Hormone.
T.A. Bicsak, C.M. Hekman, and A.J.W. Hsueh, Neuroendocrine Regulation of Oocyte Tissue Plasminogen Activator.
M.R. Brown, R. Allen, and L.A. Fisher, Assessment of Peptide Regulation of the Autonomic Nervous System.
L.H. Lazarus and W.E. Wilson, Recognition, Purification, and Structural Elucidation of Mammalian Physalaemin-Related Molecules.
M. Goedert, Radioligand Binding Assays for the Study of Neurotensin Receptors.
T.W. Moody, R.M. Kris, G. Fiskum, C.D. Linden, M. Berg, and J. Schlessinger, Characterization of Receptors for Bombesin/GRP in Human and Murine Cells.
E. Hazum, Isolation and Identification of Neuroendocrine Peptides from Milk.
M.D. Culler and A. Negro-Vilar, Passive Immunoneutralization: Regulation of Basal and Pulsatile Hormone Secretion.
W. Wetsel and A. Negro-Vilar, Combined Antibody-HPLC Approach to Assess Prohormone Processing.
K. Hermann, M.K. Raizada, M.I. Phillips, Chromatographic Methods for the Characterization of Angiotensin in Brain Tissue.
C.H. Emerson, Measurement of Thyrotropin-Releasing Hormone and Its Metabolites.
G. Valiquette and S. Neubort, Monoclonal Antibodies: Uses in Studies on Vasopressin.
J.M. Vaughan, J. Rivier, A.Z. Corrigan, R. McClintock, C.A. Campen, D. Jolley, J.K. Vogelmayr, C.W. Bardin, C. Rivier, and W. Vale, Detection and Purification of Inhibin Using Antisera Generated against Synthetic Peptide Fragments.
M. Blum, Regulation of Neuroendocrine Peptide Gene Expression.
J.E. Krause, J.D. Cremins, M.S. Carter, E.R. Brown, and M.R. MacDonald, Solution Hybridization-Nuclease Protection Assays for the Sensitive Detection of Differentially Spliced Substance P- and Neurokinin A-Encoding Messenger RNAs.
W.A. Bank and A.J. Kastin, Quantifying Carrier-Mediated Transport of Peptides from the Brain to the Blood.
J.R. Reeve, Jr. and J.H. Walsh, Characterizing Molecular Heterogeneity of Gastrin-Releasing Peptide and Related Peptides. Use of Chemical Probes.
J.D. White and E.F. LaGamma, Determination of Neuropeptide Gene Transcription in Central and Peripheral Nervous System Tissue by Nuclear Run-on Assay.
D.W. Crabb, C.D. Minth, and J.E. Dixon, Assaying the Reporter Gene Chloramphenicol Acetyltransferase.
S.W. Young, III, In Situ Hybridization Histochemical Detection of Neuropeptide mRNAs Using DNA and RNA Probes.
A. Barnea, Use of Metal Complexes in Neuroendocrine Studies.
M.C. Aguila and S.M. McCann, Methods for the Study of Somatostatin.
E. Hazum, Mapping of the GnRH-Receptor Binding Site Using Selective Chemical Modifications.
Localization of Neuroendocrine Substances:
G.R. Uhl, In Situ Hybridization: Issues with Quantitation Using Radiolabeled Hybridization Probes.
P.C. Emson, H. Arai, S. Agrawal, C. Christodoulou, and M.J. Gait, Nonradioactive Methods of in Situ Hybridization-Visualization of Neuroendocrine mRNA.
F. Baldino, Jr., M.-F. Chesselet, and M.E. Lewis, High Resolution in Situ Hybridization Histochemistry.
J.S. Schwaber, In Situ Hybridization Histochemistry Combined with Markers of Neuronal Connectivity.
A.E. Bishop and J.M. Polak, Cytochemical Techniques for Studying Diffuse Neuroendocrine System.
M.E. Lewis, W.T. Rogers, R.G. Krause II, and J.S. Schwaber, Quantitation and Digital Representation of in Situ Hybridization Histochemistry.
J.T. McCabe, R.A. Desharnais, and D.W. Pfaff, Graphical and Statistical Approaches to Data Analysis for in Situ Hybridization.
Author Index.
Subject Index.