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Biophysics and Physiology of Carbon Dioxide : Symposium Held at the University of Regensburg (FRG) April 17–20, 1979
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Editor(s):
Christian Bauer
,
Gerolf Gros
,
Heinz Bartels
Publication date
(Print):
1980
Publisher:
Springer Berlin Heidelberg
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AIMS Biophysics
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ISBN (Print):
978-3-642-67574-4
ISBN (Electronic):
978-3-642-67572-0
Publication date (Print):
1980
DOI:
10.1007/978-3-642-67572-0
SO-VID:
f09cc022-b9b0-4c9c-91a2-7f50b1e5617d
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Book chapters
pp. 3
Chemical Reactions of CO2 in Water
pp. 3
Ectoenzymes: Their Modulation and Similarity to Certain Enzymes of Intracellular Membranes
pp. 15
Facilitation of CO2 Through Layers with a Spatial Distribution of Carbonic Anhydrase
pp. 17
Ectonucleotidases of Vascular Endothelial Cells: Characterisation and Possible Physiological Roles
pp. 23
Facilitated Diffusion of CO2 and Carbonic Anhydrase Activity
pp. 27
Regulation of the Hydrolysis of Adenine Nucleotides at the Surface of Cultured Vascular Cells
pp. 35
Hydrolysis of ATP and Formation of Adenosine at the Surface of Cholinergic Nerve Endings
pp. 36
Mechanisms of Facilitated CO2 and H+ Diffusion in Protein Solutions
pp. 49
Enzymatic Characteristics and Possible Role of Synaptosomal Ecto-Adenosine Triphosphatase from Mammalian Brain
pp. 49
The Effect of Diffusion Potentials on Facilitated CO2 Diffusion
pp. 58
Evidence for Facilitated Transport of CO2 in Muscle Tissue
pp. 60
Properties and Expression of an ATP-Degrading Ectoenzyme Cascade on Human Lymphoid Cells
pp. 67
The Binding of CO2 to Human Deoxyhemoglobin: An X-Ray Study Using Low-Salt Crystals
pp. 72
Study of Ecto-5′-Nucleotidase, Ecto-ATPase, and Adenosine Deaminase Activities in Relation to Lymphoid Cell Differentiation
pp. 75
The Determination of CO2 Bound to Hemoglobin as Carbamate
pp. 89
The Properties, Structure, Function, Intracellular Localisation and Movement of Hepatic 5′-Nucleotidase
pp. 117
Ecto-5′-Nucleotidase as a Probe for the Analysis of Membrane Flow During Fluid Phase Pinocytosis
pp. 84
Phylogeny and Physiological Significance of Oxygen-Linked CO2 Binding in Hemoglobin
pp. 133
Isolation and Characterization of 5′-Nucleotidase from Avian Muscle Sources and its Interaction with Filamentous Actin
pp. 89
The Carbamate Reaction with Proteins: Observation by 13C-NMR and Evaluation of Structural Consequences
pp. 102
The Measurement of the CO2 Hb Binding Curve of Human Hemoglobin by 13C-NMR Spectrometry
pp. 147
5′-Nucleotidase in the Nervous System
pp. 106
Formation and Physiological Role of Carbamino Adducts of Angiotensin, Bradykinin, and S-Methylglucagon
pp. 165
The Role of 5′-Nucleotidases in the Heart
pp. 114
Interaction Between Hemoglobins, CO2 and Anions
pp. 179
Detection and Biochemistry of Cell Surface Protein Kinase
pp. 122
The Influence of CO2 on the First Binding Constant of Oxygen to Human Hemoglobin Ao
pp. 191
Physiological Aspects of Surface Protein Kinase Activity
pp. 133
Current Concepts of the Mechanism of Action of Carbonic Anhydrase
pp. 207
Ectoglycosyltransferase Activities During Neuronal Differentiation in Cell Cultures
pp. 151
Some Structural Aspects of Carbonic Anhydrase
pp. 216
Modulation Theory of Adhesion: Role of the Ectoenzymes Glycosidase and Glycosyltransferase
pp. 154
Primary Structure of Carbonic Anhydrases
pp. 229
Molecular Forms of Acetylcholinesterase
pp. 165
Evolution of Structure and Function in the Carbonic Anhydrase Isozymes of Mammals
pp. 238
An Ectocellular Form of Acetylcholinesterase on the Plasma Membrane of Nerve Terminals in Torpedo Electric Organ
pp. 177
Carbonic Anhydrase Activity in Intact Red Cells as Measured by Means of 18O Exchange Between CO2 and Water
pp. 246
Release of Acetylcholinesterase from Nigro-Striatal Neurons
pp. 184
Crystal Structure of Carbonic Anhydrase
pp. 257
Endopeptidase-24.11: An Ectoenzyme Capable of Hydrolysing Regulatory Peptides at the Surface of Many Different Cell Types
pp. 206
Kinetics and Mechanistic Implications of CO2 Hydration Activity of Human Erythrocyte Carbonic Anhydrases
pp. 272
Ectopeptidases Responsible for the Inactivation of Enkephalins
pp. 216
Models for Metal Ion Function and Evolution of the Catalytic Step in Carbonic Anhydrase
pp. 285
Cell Surface-Bound Leucine Aminopeptidase: Target of the Immunomodulator Bestatin
pp. 226
Consequences of Metal Ion Substitutions in Human Carbonic Anhydrase B. A Carbon-13 Nuclear Magnetic Resonance Comperative Study
pp. 294
The Intramolecular Turnover Heterogeneity, a New Property of Plasma Membrane Glycoproteins. Dipeptidylaminopeptidase IV as a Model
pp. 230
Rate-Limiting Steps in the Catalytic Action of Carbonic Anhydrase
pp. 238
The pH-Independence of Carbonic Anhydrase Activity: Apparent pKa Due to Inhibition by HSO 4 −
pp. 254
Role of Buffer in Catalysis of the Hydration of CO2 by Carbonic Anhydrase
pp. 262
35Cl and 81Br Nuclear Magnetic Resonance Studies of Carbonic Anhydrase
pp. 273
NMR Studies of Carbonic Anhydrase
pp. 285
Cl− and HCO 3 − Movements Across the Red Blood Cell Membrane
pp. 291
The Rate-Limiting Event in the Depletion of 18O from CO2 in Red Cell Suspensions
pp. 299
Kinetics of CO2 Uptake by Red Cells
pp. 306
Intravascular End-Capillary CO2-H+ Disequilibrium
pp. 315
Changes in pH and \({{\text{P}}_{C{O_2}}}\) with Time in Pulmonary Post-Capillary Blood in Cats
pp. 321
Kinetics of Acid-Base Parameters of Blood After Respiratory and Metabolic Disturbances
pp. 331
Carbonic Anhydrase in Lung Tissue
pp. 339
Pulmonary Capillary Carbonic Anhvdrase
pp. 343
Can CO2 Be Actively Eliminated by the Lungs?
pp. 351
Experimental Results on Gas-Blood CO2 Equilibrium in Lungs
pp. 353
Intracapillary CO2 Gradients
pp. 356
Contribution of Red Cell-Plasma H+ Disequilibrium to Alveolar-Blood \({{\text{P}}_{C{O_2}}}\) Differences During Rebreathing
pp. 359
Diffusion Limitation in Alveolar-Capillary CO2 Transfer in Human Lungs: Experimental Evidence from Rebreathing Equilibration
pp. 366
Physiological Consequences of Carbonic Anhydrase Inhibition During Rest and Exercise, and on the Bohr Effect
pp. 379
Placental CO2 Exchange
pp. 390
Transfer of Bicarbonate in a Hemochorial Placenta
pp. 399
Recent Developments in Carbonic Anhydrase Localization: Occurrence of Carbonic Anhydrase in Calcium-Mobilizing Tissues
pp. 406
Arguments for and Against the Histochemical Carbonic Anhydrase Test
pp. 410
Activity and Properties of Carbonic Anhydrase in Striated Muscle
pp. 419
Significance of Carbonic Anhydrase for HCO 3 − Absorption and H+ Secretion in Renal Tubules
pp. 426
Formation and Ionic Composition of Cerebrospinal Fluid: The Role of Carbonic Anhydrase
pp. 436
Autoregulation of CSF H+ Activity
pp. 439
Transients and Steady State of Chloride-Bicarbonate Relationships of Brain Extra-Cellular Fluid
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