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1.

図書

図書
Brian R. Eggins
出版情報: Chichester, West Sussex : Wiley, c2002  xxi, 273 p. ; 23 cm
シリーズ名: Analytical Techniques in the Sciences(AnTS)
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Series Preface
Preface
Acronyms, Abbreviations and Symbols
About the Author
Introduction / 1:
Introduction to Sensors / 1.1:
What are Sensors? / 1.1.1:
The Nose as a Sensor / 1.1.2:
Sensors and Biosensors--Definitions / 1.2:
Aspects of Sensors / 1.3:
Recognition Elements / 1.3.1:
Transducers--the Detector Device / 1.3.2:
Methods of Immobilization / 1.3.3:
Performance Factors / 1.3.4:
Areas of Application / 1.3.5:
Transduction Elements / 2:
Electrochemical Transducers--Introduction / 2.1:
Potentiometry and Ion-Selective Electrodes: The Nernst Equation / 2.2:
Cells and Electrodes / 2.2.1:
Reference Electrodes / 2.2.2:
Quantitative Relationships: The Nernst Equation / 2.2.3:
Practical Aspects of Ion-Selective Electrodes / 2.2.4:
Measurement and Calibration / 2.2.5:
Voltammetry and Amperometry / 2.3:
Linear-Sweep Voltammetry / 2.3.1:
Cyclic Voltammetry / 2.3.2:
Chronoamperometry / 2.3.3:
Amperometry / 2.3.4:
Kinetic and Catalytic Effects / 2.3.5:
Conductivity / 2.4:
Field-Effect Transistors / 2.5:
Semiconductors--Introduction / 2.5.1:
Semiconductor--Solution Contact / 2.5.2:
Field-Effect Transistor / 2.5.3:
Modified Electrodes, Thin-Film Electrodes and Screen-Printed Electrodes / 2.6:
Thick-Film--Screen-Printed Electrodes / 2.6.1:
Microelectrodes / 2.6.2:
Thin-Film Electrodes / 2.6.3:
Photometric Sensors / 2.7:
Optical Techniques / 2.7.1:
Ultraviolet and Visible Absorption Spectroscopy / 2.7.3:
Fluorescence Spectroscopy / 2.7.4:
Luminescence / 2.7.5:
Optical Transducers / 2.7.6:
Device Construction / 2.7.7:
Solid-Phase Absorption Label Sensors / 2.7.8:
Applications / 2.7.9:
Further Reading
Sensing Elements / 3:
Ionic Recognition / 3.1:
Ion-Selective Electrodes--Introduction / 3.2.1:
Interferences / 3.2.2:
Conducting Devices / 3.2.3:
Modified Electrodes and Screen-Printed Electrodes / 3.2.4:
Molecular Recognition--Chemical Recognition Agents / 3.3:
Thermodynamic--Complex Formation / 3.3.1:
Kinetic--Catalytic Effects: Kinetic Selectivity / 3.3.2:
Molecular Size / 3.3.3:
Molecular Recognition--Spectroscopic Recognition / 3.4:
Infrared Spectroscopy--Molecular / 3.4.1:
Ultraviolet Spectroscopy--Less Selective / 3.4.3:
Nuclear Magnetic Resonance Spectroscopy--Needs Interpretation / 3.4.4:
Mass Spectrometry / 3.4.5:
Molecular Recognition--Biological Recognition Agents / 3.5:
Enzymes / 3.5.1:
Tissue Materials / 3.5.3:
Micro-Organisms / 3.5.4:
Mitochondria / 3.5.5:
Antibodies / 3.5.6:
Nucleic Acids / 3.5.7:
Receptors / 3.5.8:
Immobilization of Biological Components / 3.6:
Adsorption / 3.6.1:
Microencapsulation / 3.6.3:
Entrapment / 3.6.4:
Cross-Linking / 3.6.5:
Covalent Bonding / 3.6.6:
Selectivity / 4:
Ion-Selective Electrodes / 4.2.1:
Others / 4.2.2:
Sensitivity / 4.3:
Range, Linear Range and Detection Limits / 4.3.1:
Time Factors / 4.4:
Response Times / 4.4.1:
Recovery Times / 4.4.2:
Lifetimes / 4.4.3:
Precision, Accuracy and Repeatability / 4.5:
Different Biomaterials / 4.6:
Different Transducers / 4.7:
Urea Biosensors / 4.7.1:
Amino Acid Biosensors / 4.7.2:
Glucose Biosensors / 4.7.3:
Uric Acid / 4.7.4:
Some Factors Affecting the Performance of Sensors / 4.8:
Amount of Enzyme / 4.8.1:
Immobilization Method / 4.8.2:
pH of Buffer / 4.8.3:
Electrochemical Sensors and Biosensors / 5:
Potentiometric Sensors--Ion-Selective Electrodes / 5.1:
Concentrations and Activities / 5.1.1:
Calibration Graphs / 5.1.2:
Examples of Ion-Selective Electrodes / 5.1.3:
Gas Sensors--Gas-Sensing Electrodes / 5.1.4:
Potentiometric Biosensors / 5.2:
pH-Linked / 5.2.1:
Ammonia-Linked / 5.2.2:
Carbon Dioxide-Linked / 5.2.3:
Iodine-Selective / 5.2.4:
Silver Sulfide-Linked / 5.2.5:
Amperometric Sensors / 5.3:
Direct Electrolytic Methods / 5.3.1:
The Three Generations of Biosensors / 5.3.2:
First Generation--The Oxygen Electrode / 5.3.3:
Second Generation--Mediators / 5.3.4:
Third Generation--Directly Coupled Enzyme Electrodes / 5.3.5:
NADH/NAD[superscript +] / 5.3.6:
Examples of Amperometric Biosensors / 5.3.7:
Amperometric Gas Sensors / 5.3.8:
Conductometric Sensors and Biosensors / 5.4:
Chemiresistors / 5.4.1:
Biosensors Based on Chemiresistors / 5.4.2:
Semiconducting Oxide Sensors / 5.4.3:
Applications of Field-Effect Transistor Sensors / 5.5:
Chemically Sensitive Field-Effect Transistors (CHEMFETs) / 5.5.1:
Ion-Selective Field-Effect Transistors (ISFETs) / 5.5.2:
FET-Based Biosensors (ENFETs) / 5.5.3:
Photometric Applications / 6:
Techniques for Optical Sensors / 6.1:
Modes of Operation of Waveguides in Sensors / 6.1.1:
Immobilized Reagents / 6.1.2:
Visible Absorption Spectroscopy / 6.2:
Measurement of pH / 6.2.1:
Measurement of Carbon Dioxide / 6.2.2:
Measurement of Ammonia / 6.2.3:
Examples That Have Been Used in Biosensors / 6.2.4:
Fluorescent Reagents / 6.3:
Fluorescent Reagents for pH Measurements / 6.3.1:
Halides / 6.3.2:
Sodium / 6.3.3:
Potassium / 6.3.4:
Gas Sensors / 6.3.5:
Indirect Methods Using Competitive Binding / 6.4:
Reflectance Methods--Internal Reflectance Spectroscopy / 6.5:
Evanescent Waves / 6.5.1:
Reflectance Methods / 6.5.2:
Attenuated Total Reflectance / 6.5.3:
Total Internal Reflection Fluorescence / 6.5.4:
Surface Plasmon Resonance / 6.5.5:
Light Scattering Techniques / 6.6:
Types of Light Scattering / 6.6.1:
Quasi-Elastic Light Scattering Spectroscopy / 6.6.2:
Photon Correlation Spectroscopy / 6.6.3:
Laser Doppler Velocimetry / 6.6.4:
Mass-Sensitive and Thermal Sensors / 7:
The Piezo-Electric Effect / 7.1:
Principles / 7.1.1:
Gas Sensor Applications / 7.1.2:
Biosensor Applications / 7.1.3:
The Quartz Crystal Microbalance / 7.1.4:
Surface Acoustic Waves / 7.2:
Plate Wave Mode / 7.2.1:
Evanescent Wave Mode / 7.2.2:
Lamb Mode / 7.2.3:
Thickness Shear Mode / 7.2.4:
Thermal Sensors / 7.3:
Thermistors / 7.3.1:
Catalytic Gas Sensors / 7.3.2:
Thermal Conductivity Devices / 7.3.3:
Specific Applications / 8:
Determination of Glucose in Blood--Amperometric Biosensor / 8.1:
Survey of Biosensor Methods for the Determination of Glucose / 8.1.1:
Aim / 8.1.2:
Determination of Nanogram Levels of Copper(I) in Water Using Anodic Stripping Voltammetry, Employing an Electrode Modified with a Complexing Agent / 8.2:
Background to Stripping Voltammetry--Anodic and Cathodic / 8.2.1:
Determination of Several Ions Simultaneously--'The Laboratory on a Chip' / 8.2.2:
Sensor Arrays and 'Smart' Sensors / 8.3.1:
Background to Ion-Selective Field-Effect Transistors / 8.3.3:
Determination of Attomole Levels of a Trinitrotoluene--Antibody Complex with a Luminescent Transducer / 8.3.4:
Background to Immuno--Luminescent Assays / 8.4.1:
Determination of Flavanols in Beers / 8.4.2:
Background / 8.5.1:
Responses to Self-Assessment Questions / 8.5.2:
Bibliography
Glossary of Terms
SI Units and Physical Constants
Periodic Table
Index
Series Preface
Preface
Acronyms, Abbreviations and Symbols
2.

図書

図書
Ugo Testa
出版情報: Noca Raton : CRC Press, c2002  559 p. ; 25 cm
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Iron Absorption
Iron and Cell Proliferation: Mechanisms and Applications in Cancer Therapy
Lactoferin
Transferrin
Transferrin Receptors
Soluble Transferrin Receptor
Alternative Iron Uptake Systems
Iron-Responsive Elements and Iron Regulatory Proteins
Ferritin
Iron Absorption
Iron and Cell Proliferation: Mechanisms and Applications in Cancer Therapy
Lactoferin
3.

図書

図書
by Timo Koski
出版情報: Dordrecht : Kluwer Academic Publishers, c2001  xvii, 391 p. ; 25 cm
シリーズ名: Computational biology series ; vol. 2
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4.

図書

図書
edited by Stefan Hohmann, Soren Nielsen, Peter Agre
出版情報: San Diego : Academic Press, c2001  xvii, 390 p., [8] p. of plates ; 24 cm
シリーズ名: Current topics in membranes ; v. 51
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Contributors
Preface
Previous Volumes in Series
Discovery of the Aquaporins and Their Impact on Basic and Clinical Physiology / Peter Agre ; Mario J. Borgnia ; Masato Yasui ; John D. Neely ; Jennifer Carbrey ; David Kozono ; Eric Beitz ; Jason Hoffer ; Virginia Leitch ; Landon S. KingChapter 1:
Pre-Aquaporin Era / I.:
The First Recognized Water Channel Protein / II.:
Other Mammalian Aquaporins / III.:
Nonmammalian Homologs / IV.:
Perspective / V.:
References
The Aquaporin Superfamily: Structure and Function / Henning Stahlberg ; Bernard Heymann ; Kaoru Mitsuoka ; Yoshinori Fuyijoshi ; Andreas EngelChapter 2:
Introduction
Two-Dimensional Crystallization of Membrane Proteins
Electron Crystallography
Atomic Force Microscopy
AQP1, The Erythrocyte Water Channel
AQP0: The Major Intrinsic Protein of Lens Fiber Cells / VI.:
Water Channel of Escherichia coli: AqpZ / VII.:
Glycerol Channel of Escherichia coli: GlpF / VIII.:
Comparison of the High-Resolution Projection Structures of GlpF and AQP1 / IX.:
Conclusion and Perspectives / X.:
Physiological Roles of Aquaporins in the Kidney / Mark A. Knepper ; Soren Nielsen ; Chung-Lin ChouChapter 3:
Water Transport along the Renal Tubule
Water Permeability along the Renal Tubule
Aquaporin-1 Facilitates Isoosmotic Fluid Transport in Proximal Tubule
Aquaporin-1 Allows Osmotic Equilibration in the Thin Descending Limb of Henle Despite Rapid Flow of Tubule Fluid
Aquaporin-1 Allows Osmotic Equilibration in the Descending Vasa Recta
Aquaporins Provide Molecular Targets for Regulation of Water Transport in the Renal Collecting Duct
Pathophysiology of Renal Aquaporins / Tae-Hwan Kwon ; Henrik Hager ; David Marples ; Jorgen FrokiaerChapter 4:
Inherited NDI and CDI
Acquired NDI
Urinary Concentrating Defects
States of Water Retention
Conclusions
Genetic and Biophysical Approaches to Study Water Channel Biology / A. S. Verkman ; Baoxue Yang ; William R. Skach ; Alok Mitra ; Yuanlin Song ; Geoffrey T. Manley ; Tonghui MaChapter 5:
Lessons from Aquaporin Knockout Mice
Biophysical Analysis of Aquaporin Function
Aquaporin Structure and Function
New Directions in Aquaporin Physiology and Biophysics
Trafficking of Native and Mutant Mammalian MIP Proteins / Peter M. T. Deen ; Dennis BrownChapter 6:
Normal Routing of MIP Proteins
Disturbed Trafficking of MIP Proteins
Aquaporins of Plants: Structure, Function, Regulation, and Role in Plant Water Relations / Maarten J. Chrispeels ; Raphael Morillon ; Christophe Maurel ; Patricia Gerbeau ; Per Kjellbom ; Ingela JohanssonChapter 7:
The Transpiration Stream
Water Movement in and between Living Tissues
Molecular Characteristics and Transport Properties of Plant Aquaporins
Subcellular Location of Plant Aquaporins
What Do the Water and Solute Transport Properties of Membranes Tell Us about the Aquaporins in Those Membranes?
The Multiple Roles of Aquaporins: How to Link Water Transport Properties to Functions at the Cellular and Tissue Level
Regulation of Aquaporin Expression and Water Transport Activity
Microbial Water Channels and Glycerol Facilitators / Gerald Kayingo ; Roslyn M. Bill ; Guiseppe Calamita ; Stefan Hohmann ; Bernard A. PriorChapter 8:
Microbial Aquaporins and Glycerol Facilitators
Transport Properties and Channel Selectivity of Microbial MIP Channels
From Primary to Quaternary Structure in Microbial MIPs
Physiological Roles
Microbial MIP Channels in Osmoregulation
Control of the Function of Microbial MIP Channels
Conclusions and Future Perspectives
Future Directions of Aquaporin Research / Chapter 9:
Identification and Characterization of New MIP Channels
Why Have So Many MIP Channels?
Analysis of the Physiological Roles of Aquaporins
Structure and Function
Aquaporins as Targets for Treatment of Human Disease
Aquaporins as Possible Targets for Genetic Engineering and Crop Improvement
Metabolic Engineering with Aquaporins
The Aquaporin Research Community
Index
Contributors
Preface
Previous Volumes in Series
5.

図書

図書
edited by Stuart L. Schreiber, Tarun M. Kapoor and Günther Wess
出版情報: Weinheim : Wiley-VCH, 2007  3 v. ; 25 cm
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Introduction / Part I:
Chemistry and Biology -- Historial and Philosophical Aspects / Gerhard Quinkert
Using Small Molecules To Explore Biology / Part II:
Using Small Molecules to Unravel Biological Mechanisms / Tarun Kapoor
Using Natural Products to Unravel Cell Biology / Craig Crews
Engineering Control Over Protein Function Using Chemistry / Kevan Shokat
Controlling Protein Function by Caged Compounds / Carsten Schultz
Transcription Control by Small-Molecules / John Koh
Controlling Protein-Protein Interactions / Virginia Cornish ; Columbia University) Controlling Protein-Protein Interactions Using Chemical Inducers and Disrupters of Dimerization ; Tim Clackson
Protein Secondary Structure Mimetics as Modulators of Protein-Protein and Protein-Ligand Interactions / Andrew Hamilton
Expanding the Genetic Code / Masahiko Sisido
Discovering Small Molecule Probes For Biological Mechanisms / Part III:
Forward Chemical Genetics / Stuart Schreiber ; Steve Haggarty
Reverse Chemical Genetics -- An Important Strategy for the Study of Protein Function in Chemical and Drug Discovery / Herbert Waldmann
Chemical Biology and Enzymology: Protein Phosphorylation as a Case Study / Phil Cole
Chemical Strategies for Activity-based Proteomics / Ben Cravatt
The Biarsenical Tetracysteine Protein Tag: Chemistry and Biological Applications / Steve Adams
Chemical Approaches to Exploit Fusion Proteins for Functional Studies / Kai Johnsson
Expanding The Scope Of Chemical Synthesis / Part IV:
Diversity-oriented Synthesis / Derek Tan
Combinatorial Biosynthesis of Polyketides and Nonribosomal Peptides / Chaitan Khosla
Expressed Protein Ligation / Tom Muir
Chemical Synthesis of Proteins and Large Bioconjugates / Phil Dawson
New Methods for Protein Bioconjugation / Matt Francis
The Search for Chemical Probes to Illuminate Carbohydrate Function / Laura Kiessling
Chemical Clydomics as Basis for Drug Discovery / Peter Seeberger
The Bicyclid Depsipeptide Family of Histone Deacetylase / A. Ganesan
Chemical Informatics / Part V:
Wombat and Wombat-Pk / Paul Clemons
Bioactivity Databases for Lead and Drug Discovery / Tudor Oprea
Drug discovery / Part VI:
Managerial Challenges in Implementing Chemical Biology Platforms / Frank Douglas
The Molecular Basis of Predicting Druggability / Andrew Hopkins ; Pfizer)
The Target Family Approach / Peter Nestler ; Sanofi-Aventis)
Chemical Biology of Kinases Studied by NMR Spectroscopy / Harald Schwalbe
The Nuclear Receptor Superfamily and Drug Discovery / Kenneth Pearce
The GPCR-7TM Receptor Target Family / Edgar Jacoby
Drugs Targeting Protein-Protein Interactions / Patrick Chene ; Novartis)
Systems Biology / Part VII:
Prediction of ADMET properties / Ulf Norinder ; AstraZeneca)
Systems Biology of the JAK-STAT Signaling Pathway / Jens Timmer
Modeling Intracellular Signal Transduction Processes / Jason Haugh
Genome-wide Gene Expression and Application to the Analysis of T-Cell Subsets in Inflammatory Diseases / Lars Rogge
Scanning the Proteome for Targets of Organic Small Molecules Using Bifunctional Receptor Ligands / Nikolai Kley
Outlook / Part VIII:
Introduction / Part I:
Chemistry and Biology -- Historial and Philosophical Aspects / Gerhard Quinkert
Using Small Molecules To Explore Biology / Part II:
6.

図書

図書
Sigel, Helmut
出版情報: New York : Marcel Dekker, c1987  xxv, 295 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 21
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Preface to the Series
Preface to Volume 21
Contributors
Contents of Other Volumes
Nuclear Relaxation Times as a Source of Structural Information / Gil Navon ; Gianni ValensinChapter 1:
Theoretical Considerations / 1.:
Applications / 2.:
Abbreviations
References
Nuclear Relaxation in NMR of Paramagnetic Systems / Ivano Bertini ; Claudio Luchinat ; Luigi MessoriChapter 2:
Nuclear Relaxation and Observability of the NMR Signals
Physical Consequences of Unpaired Electron-Nucleus Coupling
T[superscript -1 subscript 1M] and Nuclear Magnetic Relaxation Dispersion (NMRD) / 3.:
T[superscript -1 subscript 2M] / 4.:
Electron Relaxation Mechanisms / 5.:
Electron and Nuclear Relaxation in Magnetically Coupled Systems / 6.:
Concluding Remarks / 7.:
NMR Studies of Magnetically Coupled Metalloproteins / Lawrence Que, Jr. ; Michael J. MaroneyChapter 3:
Introduction
Physical Background
Superoxide Dismutase
Hemerythrin
Ribonucleotide Reductase
Uteroferrin
Ferredoxins
Summary / 8.:
Proton NMR Studies of Biological Problems Involving Paramagnetic Heme Proteins / James D. SatterleeChapter 4:
Heme Proteins
The Hyperfine Shift in Paramagnetic Heme Proteins
Resonances of the Porphyrin Ring
Resonances of Axial Ligands
Resonances of the Heme Pocket not Attributable to Heme Ligands
Proton NMR Studies of Protein-Protein Complexes
Conclusion
Metal-Porphyrin Induced NMR Dipolar Shifts and Their Use in Conformational Analysis / Nigel J. Clayden ; Geoffrey R. Moore ; Glyn WilliamsChapter 5:
Theory
Structural and Magnetic Properties of Metalloporphyrins
Conformational Analysis
Conclusions and Outlook
Relaxometry of Paramagnetic Ions in Tissue / Seymour H. Koenig ; Rodney D. Brown IIIChapter 6:
General Background
Relaxometry of Fe[superscript 3+]
Relaxometry of Mn[superscript 2+]
Relaxometry of Gd[superscript 3+]
The Present and Future
Author Index
Subject Index
Preface to the Series
Preface to Volume 21
Contributors
7.

図書

図書
Sigel, Helmut
出版情報: New York : Marcel Dekker, c1987  xxiii, 290 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 22
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8.

図書

図書
with contributions by C. Bedetti ... [et al.]
出版情報: Berlin ; Tokyo : Springer, c1987  182 p. ; 25 cm
シリーズ名: Advances in biochemical engineering/biotechnology ; 35
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9.

図書

図書
Sigel, Helmut
出版情報: New York : Dekker, c1985  xxvi, 429 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 19
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Preface to the Series
Preface to Volume 19
Contributors
Contents of Other Volumes
The Discovery of Ionophores: An Historical Account / Berton C. PressmanChapter 1:
Abbreviations
References
Tetracyclines and Daunorubicin / R. Bruce MartinChapter 2:
Introduction / 1.:
Tetracyclines / 2.:
Daunorubicin / 3.:
Interaction of Metal Ions with Streptonigrin and Biological Properties of the Complexes / Joseph HajduChapter 3:
Structural and Chemical Properties of Streptonigrin and Its Metal Complexes
Biological Activity and Suggested Mechanistic Schemes for the Antitumor Action of Streptonigrin
Conclusions / 4.:
Bleomycin Antibiotics: Metal Complexes and Their Biological Action / Yukio Sugiura ; Tomohisa Takita ; Hamao UmezawaChapter 4:
Structural and Synthetic Aspects of Bleomycin
Characteristics of Bleomycin-Metal Complexes
Oxygen Activation and Redox Cycle of the Bleomycin-Iron Complex
Interaction of Bleomycin and Its Iron Complex with DNA / 5.:
Sequence-Specific DNA Cleavage by the Bleomycin-Iron Complex / 6.:
Metal Complexes and DNA Cleavage of Bleomycin Analogs: Peplomycin, Tallysomycin, and Phleomycin / 7.:
Metal Complexes and Oxygen Activation by Synthetic Analogs and Biosynthetic Intermediates of Bleomycin / 8.:
Molecular Mechanism of Bleomycin Action / 9.:
Interaction Between Valinomycin and Metal Ions / K. R. K. Easwaran10.:
Structure and Conformation of Free Valinomycin
Structure and Conformation of Valinomycin-Metal Ion Complexes
Valinomycin-Metal Ion Complexes in Transmembrane Ion Transport
Abbreviations and Definitions
Beauvericin and the Other Enniatins / Larry K. SteinraufChapter 6:
Ion Binding
Membrane Transport
Analogs
Complexing Properties of Gramicidins / James F. Hinton ; Roger E. Koeppe IIChapter 7:
Structural Properties
Ion-Complexing Properties
Transport Properties
Nactins: Their Complexes and Biological Properties / Yoshiharu Nawata ; Kunio Ando ; Yoichi IitakaChapter 8:
Molecular Structure of Nactins
Complexes
Biological Properties
Cation Complexes of the Monovalent and Polyvalent Carboxylic Ionophores: Lasalocid (X-537A), Monensin, A23187 (Calcimycin), and Related Antibiotics / George R. PainterChapter 9:
Structure of Ionophore-Cation Inclusion Complexes
Techniques for Measuring Equilibrium Ionophore-Ion Affinities
Carboxylic Ionophore-Mediated Ion Transport
Biological Test Systems
Conformational Aspects of Ion Capture and Membrane Transport
Biological Applications of Ionophores
Overview
Complexes of D-Cycloserine and Related Amino Acids with Antibiotic Properties / Paul O'BrienChapter 10:
Mode of Action
Uses of D-Cycloserine
Organic Chemistry of D-Cycloserine
Metal Ion Coordination by D-Cycloserine
Metal Ion Coordination by D-Cycloserine Derivatives
Iron-Containing Antibiotics / J. B. Neilands ; J. R. ValentaChapter 11:
Iron(III) Complexes
Iron(II) Complexes
Miscellaneous Compounds
General Conclusions
Cation-Ionophore Interactions: Quantification of the Factors Underlying Selective Complexation by Means of Theoretical Computations / Nohad Gresh ; Alberte PullmanChapter 12:
Outline of the Methodology
Selective Binding of Alkali Cations by Valinomycin
Selective Complexation of K[superscript +], Na[superscript +], and NH[superscript + subscript 4] by Nonactin
Selective Binding of Mg[superscript 2+] and Ca[superscript 2+] by Ionophore A23187
Structural Properties of Valinomycin and A23187
Energy Profiles for Single and Double Occupancy by Na[superscript +] of the Gramicidin A Channel
Author Index
Subject Index
Preface to the Series
Preface to Volume 19
Contributors
10.

図書

図書
H.J.M. Bowen
出版情報: London ; New York : Academic Press, 1966  ix, 241 p. ; 24 cm
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