Stabilities and properties of multilinked hemoglobins.
Crosslinking of both human and dog hemoglobin has been done with a variety of reagents to produce singly, doubly and multiply crosslinked hemoglobins. Succinate and glutarate diaspirins did not crosslink deoxy human hemoglobin in good yield, in contrast to the fumarate analog (DBSF). Deoxy dog Hb did not react well with DBSF, but oxy dog Hb did react, giving crosslinked tetramers as well as dimers on SDS electrophoresis. Crosslinking with a short, rigid reagent (difluorodinitrobenzene) resulted in a similar product for both oxy and deoxy hemoglobin that had high stability and oxygen affinity. The trilinker, tris-chloroethylamine, produced a more stable product than the corresponding crosslinker, bis-chloroethylamine. Double crosslinking oxy Hb with DBSF and dimethylpimelimidate or with DBSF followed by deoxygenation and recrosslinking with DBSF gave products with higher denaturation temperatures. The diaspirin double crosslinked product had high oxygen affinity.
Olsen
K W
KW
Department of Chemistry, Loyola University of Chicago, IL 60626.
Zhang
Q Y
QY
Huang
H
H
Sabaliauskas
G K
GK
Yang
T
T
D000818:Animals; D001802:Blood Substitutes / Q000138:chemical synthesis / Q000737:chemistry*; D003432:Cross-Linking Reagents; D004285:Dogs; D004355:Drug Stability; D006454:Hemoglobins / Q000138:chemical synthesis / Q000737:chemistry*; D006801:Humans; D011489:Protein Denaturation; D013696:Temperature
D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins