Browsing by Author "Weiss, Mitchell J."

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    Alpha-hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of alpha subunits of human HbA with hydrogen peroxide
    (The American Society for Biochemistry and Molecular Biology, Inc., 2012) Mollan, Todd L.; Banerjee, Sambuddha; Wu, Gang; Siburt, Claire J.Parker; Tsai, Ah-Lim; Olson, John S.; Weiss, Mitchell J.; Crumbliss, Alvin L.; Alayash, Abdu I.
    Background: AHSP modifies redox properties of bound α subunits. Results: Isolated hemoglobin subunits exhibit significantly different redox properties compared to HbA. A significant decrease in the reduction potential of α subunits bound to AHSP results in preferential binding of ferric α. Conclusion: AHSP:α subunit complexes do not participate in ferric-ferryl heme redox cycling. Significance: AHSP binding to α subunits inhibits subunit pseudoperoxidase activity.
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    Enhancing recombinant hemoglobin production by co-expression with alpha hemoglobin stabilizing protein
    (2010-01-05) Olson, John S.; Weiss, Mitchell J.; Rice University; Children's Hospital of Philadelphia; United States Patent and Trademark Office
    The present disclosure relates to the use of AHSP to stabilize the α subunit of rHb. AHSP may be co-expressed with the hemoglobin genes. AHSP stabilization may be used to increase the production of intact rHb in various systems, such as E. coli, other microorganisms, or animal erythroid cells. This intact rHb may then be used as part of a blood substitute product.