O(2) affinity of cross-linked hemoglobins modifies O(2) metabolism in proximal tubules. |
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| Authors: | A D Baines P Ho |
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| Affiliation: | Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada. andrew.baines@utoronto.ca |
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| Abstract: | Previous experiments using cross-linked tetrameric hemoglobins (XLHb) to perfuse isolated rat kidneys showed that high-O2-affinity XLHb improved proximal tubule function more effectively than low-O2-affinity XLHb. To determine how function was improved, proximal tubule fragments were incubated with albumin, Hb34 [half-saturation point (P50) 34 Torr], or Hb13 (P50 13 Torr) with Po2 values ranging from 22 to 147 Torr. ATP content reflected O2 delivery to mitochondria. Both XLHb increased ATP, Hb34 with Po2 >or= 47 Torr and Hb13 with Po2
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