Recombinant hemoglobins as artificial oxygen carriers.
This paper describes the approaches we have taken to construct a) mutant hemoglobins with different oxygen affinities, and b) mutant hemoglobins and myoglobins that polymerize to high molecular weight aggregates in an effort to prevent extravasation and the associated vasoactivity. In vivo testing indicates that exchange transfusion of polymeric hemoglobins in mice does not result in vasoactivity and that polymeric hemoglobins are effective oxygen carriers to ischemic tissues irrespective of their oxygen affinity and cooperativity.
Fronticelli
Clara
C
Department of Anesthesiology and Critical Care Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA. cfrontic@jhmi.edu
Koehler
Raymond C
RC
Brinigar
William S
WS
D000818:Animals; D001802:Blood Substitutes / Q000737:chemistry* / Q000378:metabolism / Q000627:therapeutic use; D005078:Exchange Transfusion, Whole Blood; D006454:Hemoglobins / Q000235:genetics / Q000378:metabolism / Q000627:therapeutic use*; D007511:Ischemia / Q000628:therapy; D051379:Mice; D008970:Molecular Weight; D009154:Mutation; D009211:Myoglobin; D010100:Oxygen / Q000378:metabolism*; D011108:Polymers; D015202:Protein Engineering; D011994:Recombinant Proteins
D001802:Blood Substitutes; D006454:Hemoglobins; D009211:Myoglobin; D011108:Polymers; D011994:Recombinant Proteins; D010100:Oxygen