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1.
Protein J ; 42(3): 148-149, 2023 Jun.
Article in English | MEDLINE | ID: mdl-37198347
2.
Microvasc Res ; 64(3): 463-75, 2002 Nov.
Article in English | MEDLINE | ID: mdl-12453440

ABSTRACT

Diffusion of oxyhemoglobin has been shown to augment the oxygen transport inside the red blood cells. Measurement of hemoglobin diffusion coefficients by pulsed-field gradient (PFG) nuclear magnetic resonance (NMR) technique can be used for estimating this augmentation effect. Self-diffusion coefficients of polymerized and unpolymerized bovine hemoglobin (Hb) and several other proteins were measured using this technique. The Hb diffusion coefficient was used to determine the effective permeability of oxygen and augmentation of oxygen transport through samples of Hb solutions due to diffusion of oxyhemoglobin. The values compared well with our previous diffusion cell measurements of effective diffusivity and augmentation. Our NMR studies show that even at low concentrations the augmentation of oxygen transport due to diffusion can be significant. The PFG NMR technique can thus provide an accurate and easy method for measuring augmentation of oxygen transport, especially in dilute samples of Hb. The results on polyhemoglobin and high-molecular-weight hemoglobin are of both basic interest and practical value in assessing the promise and performance of hemoglobin-based blood substitutes.


Subject(s)
Hemoglobins/metabolism , Oxygen/metabolism , Animals , Biological Transport , Cattle , Diffusion , Hemoglobins/chemistry , Humans , Magnetic Resonance Spectroscopy , Myoglobin/chemistry , Oligochaeta , Ovalbumin/chemistry , Polymers/chemistry , Temperature
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