PubMed Health⌕ Search

PubMed · 9785073

Artificial oxygen carriers.

Abstract

The clinical availability of artificial oxygen carriers (AOCs) would result in profound alterations in transfusion medical practice. Rapid progress in the scientific and technological development of AOCs has advanced to a critical stage at which safe and effective alternatives to the transfusion of red blood cells are emerging. Haemoglobin- and perfluorocarbon-based oxygen carriers are under current clinical investigation. Artificial oxygen-carrying solutions, by virtue of their acellular structure, can be used to transport oxygen to ischaemic tissues that cannot otherwise be reached by cellular blood components. Organs awaiting transplantation can be preserved for a long time after perfusion with AOCs and tumour susceptibility to chemo- and radiotherapy is increased. The use of AOCs is therefore not confined to their use as red blood cell substitutes, but may find a wide spectrum of interdisciplinary applications.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T Frietsch, C Lenz, K F Waschke. 1998. Artificial oxygen carriers.. https://doi.org/10.1046/j.1365-2346.1998.00356.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway.

Hydrogen peroxide (H(2)O(2)) triggers a redox cycle between ferric and ferryl hemoglobin (Hb) leading to the formation of a transient protein radical and a covalent hemeprotein cross-link. Addition of H(2)O(2) to highly purified human hemoglobin (HbA(0)) induced structural changes that primarily resided within beta subunits followed by the internalization of the heme moiety within alpha subunits. These modifications were observed when an equal molar concentration of H(2)O(2) was added to HbA(0) yet became more abundant with greater concentrations of H(2)O(2). Mass spectrometric and amino acid analysis revealed for the first time that betaCys-93 and betaCys-112 were oxidized extensively and irreversibly to cysteic acid when HbA(0) was treated with H(2)O(2). Oxidation of further amino acids in HbA(0) exclusive to the beta-globin chain included modification of betaTrp-15 to oxyindolyl and kynureninyl products as well as betaMet-55 to methionine sulfoxide. These findings may therefore explain the premature collapse of the beta subunits as a result of the H(2)O(2) attack. Analysis of a tryptic digest of the main reversed phase-high pressure liquid chromatography fraction revealed two alpha-peptide fragments (alpha128-alpha139) and a heme moiety with the loss of iron, cross-linked between alphaSer-138 and the porphyrin ring. The novel oxidative pathway of HbA(0) modification detailed here may explain the diverse oxidative, toxic, and potentially immunogenic effects associated with the release of hemoglobin from red blood cells during hemolytic diseases and/or when cell-free Hb is used as a blood substitute.

Blood Substitutes↗

Water solubility in linear fluoroalkanes used in blood substitute formulations.

The interactions between water and n-perfluoroalkanes or substituted alpha-(omega-)fluoroalkanes used in blood substitute formulations were investigated experimentally and using ab initio calculations. The solubility of water in C(6)-C(9) perfluoroalkanes and five C(8) analogues of substituted fluoroalkanes was measured in the temperature range between 288 and 318 K at atmospheric pressure, using a Karl Fischer coulometer. From these data, the thermodynamic functions and partial molar solvation quantities such as Gibbs energy, enthalpy, and entropy were determined and compared with the interaction energies in 1:1 water-fluoroalkane complexes in vacuum, obtained using B3LYP/6-311++G(d,p). The experimental solubility data indicates a significant specific interaction between the water and the alpha-(omega-)substitute atom (H, I, Br, or Cl) in the fluoroalkanes.

Blood Substitutes↗