Myoglobin and hemoglobin rotational diffusion in the cell.

Abstract:

:The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Wang D,Kreutzer U,Chung Y,Jue T

doi

10.1016/S0006-3495(97)78305-X

subject

Has Abstract

pub_date

1997-11-01 00:00:00

pages

2764-70

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(97)78305-X

journal_volume

73

pub_type

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