Biophysics and Physiology of Carbon Dioxide: Symposium Held by W. Knoche (auth.), Professor Dr. Christian Bauer, Professor

By W. Knoche (auth.), Professor Dr. Christian Bauer, Professor Dr. Gerolf Gros, Professor Dr. Heinz Bartels (eds.)

This quantity includes the papers awarded on the symposium on Biophysics and body structure of Carbon Dioxide held at Regensburg, April 17-20, 1979. The manuscripts symbolize the entire or maybe a longer account of the oral shows. we now have made up our minds to not comprise any a part of the discussions which happened after the lectures simply because this may have ended in an undue expansion of the already huge quantity. The symposium introduced jointly a few 60 scientists of varied disciplines together with biophysicists, chemists, biochemists, physiologists, pharmacologists, in addition to clinicians whose examine actions are cen­ tered round the a variety of elements of the reactions and the regulatory function of CO in the physique. 2 In view of the truth that various textbooks and court cases of Symposia deal expertly with the position of CO in acid-base stability, it 2 was once made up our minds to not comprise this point within the current symposium. This holds additionally for the biochemistry of carboxylation and decarboxylation reactions. specific emphasis was once put on the next topics: (1) Chemical reactions of CO in water and facilitated diffusion of CO2 , 2 (2) CO adducts to proteins, particularly hemoglobin, and peptide 2 hormones, (3) constitution and serve as of carbonic anhydrase, (4) CO 2 alternate and carbonic anhydrase job in respiration and nonrespi­ ratory platforms. every one part comprises not less than one introductory paper that offers the present wisdom in a extra normal framework.

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Extra resources for Biophysics and Physiology of Carbon Dioxide: Symposium Held at the University of Regensburg (FRG) April 17–20, 1979

Example text

Observed proton flux by rotation as a fraction of the maximal proton flux by rotation, chemical relaxation time, rotational relaxation time, and molecular radius of the buffers used in this study: phosphate, myoglobin, human hemoglobin, and earthworm hemoglobin. The chemical relaxation times are calculated for the concentrations indicated assuming the forward velocity constant of the proton exchange reaction (see Fig. 6) to be 10 9 l/mol/s, and assuming that the experimentally determined buffer capacities of the proteins are represented by buffering groups whose pK is identical to the pH existing in the layer.

At low hemoglobin concentrations, 5-10 g%, postulated and translational diffusivities are almost identical. Here, the contribution of rotational diffusion seems to be also very small. 5 g%, however, postulated and translational diffusion coefficients are significantly different. This may be 44 G. Gros eta!. eD:! 701CJ5 (with Q2% carbonic anhydrase) DeD:! 301cP 30 Myoglobin concentration (g 11ooml) pC02 2-3Torr 10 c 20 30 Hemoglobin concentration (g/100ml) Fig. 4 a-c_ Demonstration of facilitated CO2 diffusion in various buffer solutions.

We examined the facilitated transport of CO 2 in two membrane configurations featuring an immobilized liquid membrane . In the first , the bicarbonate solution was sandwiched as a thin layer between highly permeable polymer films. In these membranes we measured the facilitated flux due to the uncatalyzed reactions, as well as the catalytic effect of CA in homogeneous solution and bound to the supporting polymer films. In the second set of experiments, analogous measurements were made using Millipore filters impregnated with bicarbonateenzyme solution and cross-linked protein membranes containing enzyme and bicarbonate.

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