Thermal stabilities of hemoglobins crosslinked with different length reagents.
Bis(3,5-dibromosalicyl) succinate and glutarate were used to crosslink met-, oxy- and deoxyhemoglobins. The added flexibility of these reagents compared to the fumarate analog resulted in a more heterogeneous product but did not greatly affect the maximum thermal stability of the crosslinked hemoglobins.
Huang
H
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Department of Chemistry, Loyola University of Chicago, IL 60626.
Olsen
K W
KW
D001241:Aspirin / Q000031:analogs & derivatives; D001802:Blood Substitutes / Q000737:chemistry* / Q000302:isolation & purification; D003432:Cross-Linking Reagents; D004355:Drug Stability; D006441:Hemoglobin A / Q000737:chemistry / Q000302:isolation & purification; D006454:Hemoglobins / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D006801:Humans; D010108:Oxyhemoglobins / Q000737:chemistry / Q000302:isolation & purification; D011489:Protein Denaturation
D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins; D010108:Oxyhemoglobins; C021630:bis(3,5-dibromosalicyl)fumarate; C021631:bis(3,5-dibromosalicyl)succinate; C036858:bis(3,5-dibromosalicyl)glutarate; C100003:deoxyhemoglobin; D006441:Hemoglobin A; C029774:oxyhemoglobin A; D001241:Aspirin