摘要
探讨人肝脏血红素加氧酶（ＨＯ）同功酶的性质，并应用血红素加氧酶抑制剂锡－原卟啉（ＳｎＰＰ）抑制酶的活性，为临床新生儿黄疸的防治提供新途径。方法采用２－二乙氨乙基－葡聚糖凝胶Ａ－２５和羟基磷灰石柱层析法从人肝脏分离纯化ＨＯ的同功酶，进行酶活性检测和十二烷基磺酸钠－聚丙烯酰胺凝胶电泳分析。结果人肝脏微粒体含ＨＯ的同功酶，按洗脱先后顺序分别得到分子量为３００００和３６０００的ＨＯ－１和ＨＯ－２。酶促反应中需相同辅酶参与，其中ＨＯ－１酶活性明显高于ＨＯ－２，两者之比为２．４１，从分子量和酶的催化活性分析，发现ＨＯ－１属诱导型的传统ＨＯ同功酶，ＨＯ－２为新发现的非诱导型ＨＯ的同功酶。结论ＳｎＰＰ能有效抑制ＨＯ－１的活性，使胆红素产生减少。
Objective The purification and identification of heme oxygenase isoforms (HO 1) and HO 2 from human liver were described and Sn protoporphyrin (SnPP) was used to inhibit HO 1 activity in order to provide a new method for prevention and treatment of neonatal jaundice. Methods Human hepatic microsomal fractions were purified by DEAE Sephadex A 25 and hydroxylapatite chromatography. The enzyme activities of the two isoforms were detected with and without SnPP. Results HO 1 was the predominant form with a ratio of 2.4∶1 (HO 1∶HO 2). The apparent molecular weight of HO 1 and HO 2 on SDS PAGE was 30,000 and 36,000 under reducing conditions, respectively. The study also showed that HO 1 was the traditional inducible heme oxygenase and HO 2 was a non inducible heme oxygenase. Conclusion The efficient inhibition effect of SnPP on HO 1 is suggested.
出处
《中华医学杂志》
CAS
CSCD
北大核心
1997年第2期126-129,共4页
National Medical Journal of China
基金
国家自然科学基金
