Hemoglobin-superoxide dismutase-chemical linkages that create a dual-function protein.
Chemical reagents were designed to cross-link and connect hemoglobin and superoxide dismutase, combining the oxygen transport and superoxide-removal capabilities of the red cell in a dual-function protein. Reaction of 1 with thiol-protected hemoglobin followed by reduction produces cross-linked hemoglobin with a free thiol on the cross-link. Reaction of SOD with 5 produces a cross-linked protein with a maleimide on the cross-link. Addition of the hemoglobin-thiol to the SOD-maleimide produces a protein with the desired dual properties. Hemoglobin's oxygenation cooperativity is lowered as a result of being in the conjugate, while SOD's activity is equal to that of the native protein.
Alagic
Amer
A
Contribution from Davenport Laboratories, Department of Chemistry, University of Toronto, Toronto, Canada, M5S 3H6.
Koprianiuk
Agnieszka
A
Kluger
Ronald
R
D003432:Cross-Linking Reagents / Q000138:chemical synthesis / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008301:Maleimides / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D013482:Superoxide Dismutase / Q000737:chemistry* / Q000378:metabolism
D003432:Cross-Linking Reagents; D006454:Hemoglobins; D008301:Maleimides; C043592:maleimide; D013482:Superoxide Dismutase