TRIS(3,5-DIBROMOSALICYL) TRICARBALLYLATE CROSS-LINKED HEMOGLOBIN - FUNCTIONAL-EVALUATION

Both oxy and deoxy human hemoglobin A were crosslinked with tris(3,5-d ibromosalicyl) tricarballylate. The major species from both reactions contained an inter-subunit crosslink. The denaturation transition (T-m ) of the oxy crosslinked hemoglobin increased 14.5 degrees C and that of deoxy crosslinked hemoglobin, 13.0 degrees C. The apparent rare con stant (k(app)) of autoxidation for oxy crosslinked hemoglobin remained the same as native hemoglobin but that of the deoxy crosslinked hemog lobin increased by 34%. The higher oxygen affinity and lower cooperati vity of the crosslinked proteins compared with native hemoglobin indic ated that the crosslink shifted the conformation to the R state.