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Chemically modified and recombinant hemoglobin blood substitutes.

S R Snyder, J A Walder

    Biotechnology (Reading, Mass.)
    |January 1, 1991
    PubMed
    Summary

    Chemically modified hemoglobins show promise as blood substitutes, with HbXL99 alpha being heat-stable for viral inactivation. Future developments aim for longer retention times and scalable production, potentially using transgenic animals.

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    Area of Science:

    • Biochemistry
    • Biotechnology
    • Hematology

    Background:

    • Development of cross-linked hemoglobins as potential blood substitutes.
    • HbXL99 alpha demonstrates heat stability for viral inactivation, enabling human blood as a source material.
    • Preliminary studies show promise for HbXL99 alpha in cardiac perfusion during angioplasty.

    Purpose of the Study:

    • To review the development and properties of intramolecularly cross-linked hemoglobins for blood substitute applications.
    • To discuss the potential for large-scale production and therapeutic use of modified hemoglobins.
    • To explore future directions in hemoglobin engineering and production.

    Main Methods:

    • Chemical cross-linking of hemoglobin to create derivatives with improved properties.
    • Assessment of heat stability for viral inactivation.
    • Expression of human hemoglobin in microbial (E. coli) and transgenic animal systems.
    • Evaluation of preliminary therapeutic applications.

    Main Results:

    • Several cross-linked hemoglobin derivatives, including HbXL99 alpha, have been developed with potential as blood substitutes.
    • HbXL99 alpha is heat-stable, allowing for viral inactivation and use of human blood.
    • Recombinant human hemoglobin production achieved in E. coli and transgenic mice.
    • Potential for transgenic pigs or cows to produce human hemoglobin and other valuable proteins.

    Conclusions:

    • Cross-linked hemoglobins, particularly HbXL99 alpha, offer viable options for blood substitutes due to their stability and production potential.
    • Engineering hemoglobin through recombinant DNA technology and transgenic systems can tailor properties for specific applications.
    • Future research should focus on developing cross-linking agents for longer intravascular retention and optimizing large-scale production, potentially in transgenic animals, to ensure future blood supply needs.

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