| Literature DB >> 10867702 |
J Wolber1, A Cherubini, M O Leach, A Bifone.
Abstract
The spin-lattice relaxation time, T(1), of hyperpolarized (129)Xe in blood is sensitive to blood oxygenation. In particular, it has been shown that (129)Xe T(1) is shorter in venous blood than in arterial blood. We have studied the T(1) of hyperpolarized (129)Xe dissolved in human blood as a function of blood oxygenation level, sO(2), in the physiological oxygenation range. We show that the (129)Xe relaxation rate, T(1)(-1), varies in a nonlinear fashion as a function of sO(2). This finding suggests that direct interaction of xenon with the paramagnetic heme group of deoxyhemoglobin is not the dominant oxygenation-dependent relaxation mechanism for (129)Xe in blood. These results corroborate the idea that the oxygenation-dependence of (129)Xe T(1) is determined by conformational changes of hemoglobin induced by oxygen binding. Copyright 2000 John Wiley & Sons, Ltd.Entities:
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Year: 2000 PMID: 10867702 DOI: 10.1002/1099-1492(200006)13:4<234::aid-nbm632>3.0.co;2-k
Source DB: PubMed Journal: NMR Biomed ISSN: 0952-3480 Impact factor: 4.044