The functional properties of hemoglobin modified with mellitic dianhydride: possible applications as a blood substitute.
Human oxyhemoglobin reacts with mellitic dianhydride to produce a modified protein which shows a reduced oxygen affinity over a wide pH range, a reduced but significant cooperativity, a reduced Bohr effect and no response to the allosteric effectors: chloride, clofibric acid or inositol hexaphosphate. The amount of crosslinking in the modified hemoglobin is approximately 22% suggesting promise as a blood substitute. Reaction of deoxyhemoglobin with mellitic dianhydride produces a modified protein with reduced response to clofibric acid and a decrease in oxygen affinity in the presence of inositol hexaphosphate.
Currell
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Department of Chemistry and Biochemistry, California State University, Los Angeles 90032.
Chow
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Yimenu
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D001802:Blood Substitutes / Q000138:chemical synthesis*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D015394:Molecular Structure; D010100:Oxygen / Q000097:blood; D010796:Phthalic Anhydrides / Q000737:chemistry*; D013461:Sulfur Oxides / Q000737:chemistry*
D001802:Blood Substitutes; D006454:Hemoglobins; D010796:Phthalic Anhydrides; D013461:Sulfur Oxides; C081897:mellitic dianhydride; C023589:thionyl chloride; D010100:Oxygen