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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 301 (1968), S. 302-310 
    ISSN: 1432-2013
    Keywords: Bohr shift ; Rapidity of CO2 Exchange ; Carbonic Anhydrase ; Kinetics of Hemoglobin ; Bohr-Effekt ; Geschwindigkeit des CO2-Austausches ; Carboanhydrase ; Reaktionskinetik des Hämoglobins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird der zeitliche Ablauf des Bohr-Effektes an dünnen Blutlamellen, bestehend aus einer einlagigen Erythrocytenschicht mit beidseitigem Plasmarand, untersucht. Die einer plötzlichen Änderung des CO2-Druckes folgende O2-Sättigungsänderung des Hämoglobins wird bei 37° C im Bereich zwischen $$S_{{\text{O}}_{\text{2}} } = 83\% $$ und 49% in beiden Richtungen durchgeführt und photometrisch analysiert. Dabei ergibt sich: 1. Die Zeit für den Anstieg der O2-Sättigung der Blutlamelle ist etwa sechsmal länger als die für die O2-Entsättigung. Die mittleren Halbwertzeiten betragen 0,97 bzw. 0,17 sec. 2. Der O2-Entsättigungsvorgang nach einer CO2-Druckerhöhung benötigt fast die gleiche Zeit wie die im selben Bereich ablaufende Entsättigung nach einer O2-Druckerniedrigung. Daraus folgt, daß die O2-Diffusionsrate den CO2-Austausch in dieser Richtung zeitlich begrenzen kann. 3. Der längere O2-Aufsättigungsprozeß nach einer CO2-Druckerniedrigung hängt in seinem zeitlichen Ablauf von der Menge des ausgetauschten HCO 3 − ab. Bei größeren CO2-Sprüngen kann die Hamburger-Shift den Bohr-Effekt zeitlich begrenzen.
    Notes: Summary The time course of the Bohr effect on thin blood lamellas, consisting of a single layer of erythrocytes with a plasma layer on both sides, is examined. The O2 saturation change of the hemoglobin, following a sudden change in the CO2 pressure, is carried out in both directions at a temperature of 37° C, within the range $$S_{{\text{O}}_{\text{2}} } = 83\% $$ and 49%, and photometrically analyzed. The analysis shows that: 1. The time needed for the increase in the O2 saturation of the blood lamellas is approximately 6 times greater than that required by the O2 desaturation process. The average half-value times are 0.97 sec and 0.17 sec, respectively. 2. The O2 desaturation process, following a CO2 pressure increase, needs almost as much time as a desaturation process in the same range, after an O2 pressure decrease. Hence, it follows that the O2 diffusion rate can temporally limit the CO2 exchange in this direction. 3. After a CO2 decrease, the time course of the longer O2 saturation process depends on the quantity of HCO 3 − inside the erythrocyte. When there is a considerable CO2 jump, the Hamburger shift can temporally limit the Bohr effect.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 78 (1966), S. 595-596 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The complex dielectric constant of aqueous hemoglobin solution was measured at 9.5 GHz. A microwave technique allowing phase and attenuation settings with an accuracy of 0.3° and 0.03 db was used. The shift of the relaxation wavelength and the hydration values of horse hemoglobin were determined for native and lyophilized hemoglobin solution and erythrocytes suspensions as well. The isotope effect of light and heavy water on these parameters was detected. The influence of buffers was studied. Relative measurements, with the sensitivity increased by a factor of 20, were made with alternating oxygenated and deoxygenated human hemoglobin solutions. The oxygenation of hemoglobin was found to leave the hydrated molecule volume invariant within ±250 Å3, while a shift of the relaxation wavelength of 0.0025 ± 0.0015 cm occurs for a hemoglobin concentration of 107 g/l. The results are discussed in terms of the structure and function interrelationship of hemoglobin and the current picture of water structure.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Dielectric dispersion measurements with aqueous solutions of hemoglobin and myoglobin have been performed in the frequency range from 100 kcps to 15 Mcps. The influence of preparation, particle size, and solvent conditions was studied. The results are analyzed in terms of an orientational polarization mechanism.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 586-586 
    ISSN: 0570-0833
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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