富马酸双（3,5-二溴水杨酸）交联对血红蛋白自氧化的影响。

The effect of crosslinking by bis(3,5-dibromosalicyl) fumarate on the autoxidation of hemoglobin.

作者信息

Yang T, Olsen K W

机构信息

Department of Chemistry Loyola University of Chicago, IL 60626.

出版信息

Biochem Biophys Res Commun. 1989 Sep 15;163(2):733-8. doi: 10.1016/0006-291x(89)92284-5.

DOI:10.1016/0006-291x(89)92284-5

PMID:2783118

Abstract

Bis(3,5-dibromosalicyl) fumarate was used to crosslink hemoglobin both in the oxy and deoxy states. This double headed diaspirin was known to crosslink oxy Hb A selectively between Lys 82 beta 1 and Lys 82 beta 2 (Walder, J. A., et al. (1979) Biochemistry 18, 4265) and deoxy Hb A between Lys 99 alpha 1 and Lys 99 alpha 2 (Chatterjee R. Y., et al. (1986) J. Biol. Chem. 261, 9929). The autoxidation at 37 degrees C of oxy alpha 99 crosslinked hemoglobin was found to be 1.8 times as fast as that of Hb A while that of the oxy beta 82 crosslinked hemoglobin was only 1.2 times as fast. After 5 hours the formation of methemoglobin in the alpha crosslinked Hb A is 21.3% compared to 10.8% in beta crosslinked Hb A and 6.4% in Hb A. These results may effect the proposed use of alpha 99 crosslinked hemoglobin as a blood substitute by demonstrating the need for protection from autoxidation during storage.

摘要

富马酸双（3,5 - 二溴水杨酸）酯用于在氧合和脱氧状态下交联血红蛋白。已知这种双头二阿司匹林能选择性地使氧合血红蛋白A在β1链的赖氨酸82和β2链的赖氨酸82之间交联（瓦尔德，J.A.等人（1979年）《生物化学》18卷，4265页），并使脱氧血红蛋白A在α1链的赖氨酸99和α2链的赖氨酸99之间交联（查特吉，R.Y.等人（1986年）《生物化学杂志》261卷，9929页）。发现37℃下氧合α99交联血红蛋白的自氧化速度是血红蛋白A的1.8倍，而氧合β82交联血红蛋白的自氧化速度仅为血红蛋白A的1.2倍。5小时后，α交联血红蛋白A中高铁血红蛋白的形成率为21.3%，相比之下，β交联血红蛋白A中的高铁血红蛋白形成率为10.8%，血红蛋白A中的高铁血红蛋白形成率为6.4%。这些结果可能会影响将α99交联血红蛋白用作血液替代品的提议，因为这表明在储存期间需要防止自氧化。