ENHANCED OXIDATION OF BIS(3,5-DIBROMOSALICYL) FUMARATE ALPHA-ALPHA CROSS-LINKED HEMOGLOBIN BY FREE-RADICALS GENERATED BY XANTHINE/XANTHINE OXIDASE

被引：2
|
作者：
SAMAJA, M
MOTTERLINI, R
ROVIDA, E
机构：
[1] Department of Biomedical Science and Technology, Scientific Institute San Raffaele, University of Milano, Olgettina 60
来源：
ARTIFICIAL CELLS BLOOD SUBSTITUTES AND BIOTECHNOLOGY | 1994年 / 22卷 / 03期
关键词：
D O I：
10.3109/10731199409117879
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The xanthine/xanthine oxidase reaction produces reproducible amounts of oxygen-derived free radicals that oxidize human oxyhemoglobin (Hb). We monitored the kinetics of the oxidation of stripped Hb (sHb), purified HbA(0) and a-a cross-linked Hb (HbXL99 alpha) at [Hb] in the 5 to 150 mu M (heme) range. For increasing [Hb], the oxidation halftime (t(1/2)) increased for all Hbs, but t(1/2) was always less for HbXL99 alpha than for HbA(0) and sHb. Such feature was attributed to the lower affinity for O-2 of HbXL99 alpha and may represent a serious problem for use of this Hb as blood substitute.
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页码：517 / 524
页数：8
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