I t has long been assumed that the effect of temperature on the diffusion coefficient D , the sedimentation coefficient s , and other hydrodynamic parameters is correctly described by Walden's rule and its extensions, i.e., hydrodynamic properties of dilute solutions of macromolecules scale linearl
Pulsed field gradient nmr determination of the temperature dependence of the tracer diffusion coefficient of hemoglobin
β Scribed by Cherie H. Everhart; Charles S. Johnson Jr.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1982
- Tongue
- English
- Weight
- 339 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Abstract
We have studied the temperature dependence of the tracer diffusion coefficient of carbonmonoxy hemoglobin A (HbAβCO) by means of pulsedβfield gradient nmr (PFGβnmr). Measurements were made over the temperature range from 15 to 35Β°C for samples having concentrations 7.4 and 16.7 g/dL. No significant deviations were found from the predictions of the StokesβEinstein relation. Thus, this work does not corroborate the recently proposed conformational change in hemoglobin at 22Β°C. The advantages of PFGβnmr for the study of hemoglobin are discussed.
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