Zheng Y, Olsen K W
Department of Chemistry, Loyola University of Chicago, Chicago, IL 60626, USA.
Artif Cells Blood Substit Immobil Biotechnol. 1996 Nov;24(6):587-98. doi: 10.3109/10731199609118884.
Both oxy and deoxy human hemoglobin A were crosslinked with tris(3,5-dibromosalicyl) tricarballylate. The major species from both reactions contained an inter-subunit crosslink. The denaturation transition (Tm) of the oxy crosslinked hemoglobin increased 14.5 degrees C and that of deoxy crosslinked hemoglobin, 13.0 degrees C. The apparent rate constant (kapp) of autoxidation for oxy crosslinked hemoglobin remained the same as native hemoglobin but that of the deoxy crosslinked hemoglobin increased by 34%. The higher oxygen affinity and lower cooperativity of the crosslinked proteins compared with native hemoglobin indicated that the crosslink shifted the conformation to the R state.
氧合和脱氧人血红蛋白A均与三（3,5-二溴水杨酸）三羧酸交联。两个反应的主要产物都含有亚基间交联。氧合交联血红蛋白的变性转变温度（Tm）升高了14.5摄氏度，脱氧交联血红蛋白的变性转变温度升高了13.0摄氏度。氧合交联血红蛋白的自氧化表观速率常数（kapp）与天然血红蛋白相同，但脱氧交联血红蛋白的自氧化表观速率常数增加了34%。与天然血红蛋白相比，交联蛋白具有更高的氧亲和力和更低的协同性，这表明交联使构象转变为R态。
