Oxygen affinity of hemoglobin solutions modified by coupling with NFPLP and the effects on tissue oxygenation in the isolated perfused rat liver.

Abstract:

:From these liver perfusions with Hb and Hb/HbNFPLP solutions the following conclusions can be drawn: In spite of the chemical modification of the hemoglobin molecule, no rheological differences are seen. All parameters measured were sensitive to hypoxia induced by a decrease in perfusion flow rate. The NFPLP-induced decrease in oxygen affinity was reflected in a higher venous PO2. These in-vivo observations are in agreement with the in-vitro measured oxygen dissociation curves. The difference in PO2 did not result in a change in the other oxygen-sensitive parameters in this model under the chosen conditions. Possible causes for these observations are: the level of hypoxia was too low the oxygen supply in the perfusions with the modified hemoglobin solutions was lower than the oxygen supply in the perfusions with normal hemoglobin. Whether or not this observation is due to an intrinsic property of the modified hemoglobin molecule remains to be established.

journal_name

Adv Exp Med Biol

authors

van der Plas J,Bleeker WK,de Vries-van Rossen A,van Hamersveld A,Rigter G,Loos JA,Bakker JC

doi

10.1007/978-1-4684-3291-6_48

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

473-83

eissn

0065-2598

issn

2214-8019

journal_volume

191

pub_type

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