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 complete 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 tremendous quantity. The symposium introduced jointly a few 60 scientists of assorted disciplines together with biophysicists, chemists, biochemists, physiologists, pharmacologists, in addition to clinicians whose examine actions are cen tered round the quite a few points of the reactions and the regulatory position of CO in the physique. 2 In view of the truth that a variety of textbooks and lawsuits of Symposia deal expertly with the position of CO in acid-base stability, it 2 was once made up our minds to not contain this point within the current symposium. This holds additionally for the biochemistry of carboxylation and decarboxylation reactions. specific emphasis used to be put on the next topics: (1) Chemical reactions of CO in water and facilitated diffusion of CO2 , 2 (2) CO adducts to proteins, specifically hemoglobin, and peptide 2 hormones, (3) constitution and serve as of carbonic anhydrase, (4) CO 2 trade and carbonic anhydrase task in respiration and nonrespi ratory platforms. each one part comprises at the least one introductory paper that provides the present wisdom in a extra common 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
W. W. W. 65,000). The results are shown in Figs. 4 a-c. There is clear evidence for facilitated diffusion of CO 2 in all these systems: In the case of phosphate the CO 2 diffusion coefficient (measured at boundary pC0 2 values of ~ 30 and 60 torr) is significantly greater in the presence than in the absence of carbonic anhydrase (Fig. , 1976). For myoglobin (Fig. 4b) and hemoglobin (Fig. 4c), facilitated diffusion is demonstrated by the much larger CO 2 diffusivities found at low boundary pC0 2 values as compared to those measured at high pC0 2 values.
0 indicate the directly measured translational diffusion coefficients of earthworm hemoglobin, Dtrans (quoted from Gros, 1978); • represent the protein diffusivities that have to be postulated to explain the facilitated CO 2 fluxes measured in earthworm hemoglobin solutions (see Fig. 2). 15. The standard errors of Dtrans range from 1% to 6% (n = 9 -20). 55 010- 7 cm 2 s- 1 for Dpost G. Gros eta!. 2 Proton Transport by Rotational Protein Diffusion Several years ago Moll (1962) and Wyman (1966) discussed rotational protein diffusion as a possible mechanism of facilitated oxygen diffusion in hemoglobin solutions.
We asked now whether a combination of rotational and translational diffusion of earthworm hemoglobin can quantitatively explain our experimental data. We therefore derived an equation that describes facilitated proton transport by rotational diffusion, and we measured the rotational diffusion coefficient of earthworm hemoglobin. Proton flux by rotational diffusion of a spherical protein is given by Gros (1976) and Gros et al. (I 980): (8) where r is the molecular radius of the protein, and E> its rotational diffusion coefficient.