Xia Z, Yu S C, Li Y
Ruijin Hospital Shanghai Second Medical University.
Zhonghua Yi Xue Za Zhi. 1997 Feb;77(2):126-9.
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.
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.
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.
The efficient inhibition effect of SnPP on HO-1 is suggested.
描述从人肝脏中纯化和鉴定血红素加氧酶同工型（HO-1）和HO-2，并使用锡原卟啉（SnPP）抑制HO-1活性，为新生儿黄疸的防治提供新方法。
通过DEAE-葡聚糖A-25和羟基磷灰石层析纯化人肝微粒体部分。在有和没有Snpp的情况下检测两种同工型的酶活性。
HO-1是主要形式，比例为2.4:1（HO-1:HO-2）。在还原条件下，SDS-PAGE上HO-1和HO-2的表观分子量分别为30,000和36,000。研究还表明，HO-1是传统的诱导型血红素加氧酶，HO-2是一种非诱导型血红素加氧酶。
提示SnPP对HO-1有有效的抑制作用。
