摘要
将β－环糊精（β－ＣＤ）２位羟基选择性磺酰化后，再用ＮａＨＳｅ处理使谷胱甘肽过氧化物酶（ＧＰＸ）的催化基团－ＳｅＨ引入β－ＣＤ的２位上，经空气氧化得到了ＧＰＸ模拟物双硒桥联β－环糊精．利用元素分析、核磁共振、红外光谱对此模拟物进行了表征．Ｘ光电子能谱技术测定了模拟物中硒的价态和含量．测活结果表明模拟物的ＧＰＸ活性是ＰＺ５１的７．
The artificial imitation of glutathione peroxidase is very important because of its antioxidative property for medicine.To develop an enzyme model on the basis of the ability of cyclodextrin to bind substrates, SeH was introduced on 2 position of β cyclodextrin by regioselective tosylation of 2 hydroxyl on the secondary side of β cyclodextrin and nucleophilic substitution of NaHSe, then oxidized in air,and finally a GPX mimic,2 biselenium bridged cyclodextrins (2 β CD Se Se β CD) were achieved.The mimic was analyzed by elemental analysis, IR and 1H NMR.The Se content and valence were determined by X ray photoelectron spectrum.The Se3d electron binding energy of the mimic was 54.8eV.It approached the binding energy of 55.1 eV of SeCyss,indicating the Se in mimic presented at biselenium bridged form ( Se Se ).This proved the selenium valence of mimic was 1.The experiment gave the C/Se,which was 42.8∶1 (calculated 42∶1),indicating 2 mol Se per mole mimic.The GPX activity was 7.4 U/μmol.Its activity was 7.5 times more than that of PZ51.
出处
《中国生物化学与分子生物学报》
CAS
CSCD
1999年第1期102-104,共3页
Chinese Journal of Biochemistry and Molecular Biology
关键词
Β-环糊精
模拟酶
硒
GPX
β Cyclodextrin, Glutathione peroxidase, Imitating enzyme, Selenium
