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《CHEMICAL RESEARCH IN CHINESE UNIVERSITIES》 1997-10
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Study on Immobilized Supramolecular inclusion Complex of Iron-Porphyrin as an Analogue for Peroxide Proteinase

MAO Lu-Yuan; ZHU Min; HUANG Xue-Met; SHEN Han-Xi(Department of Chemistry, Nankai University, Tianjin, 300071)LI Rong(Tianjin Commerical College, Tianjin, 300400)  
The Supramolecular inclusion complex of iron-5, 10, 15, 20-tetrakis[4-sulfophenyl]-21H, 23H-porphin (FeTPPS4 ) with p-cyclodextrin cross-linking polymer(β-CDP) was obtained and used as an analogue for peroxide proteinase. The effects of variedfactors on formation constant of the inclusion complex were investigated. The mechanism ofimmobilized supramolecular complex catalyzing p-chlorophnic acid by hydrogen peroxide wasstudied in detail. The immobilized inclusion complex as mimests of horseradish peroxidasewas very stable and found to exhibit the high proteinase-like activity, which have beendemonstrated by enzymatic methods of analysis. The method was applied to determinehydrogen peroxide with 4-aminoantipyrine and p-chlorophenic acid. The calibration curve forabsorbance-concentration(H2O2) was linear from O to 3. 0 μg/mL and the linear correlationcoefficient was 0. 999 4.
【Fund】: 国家自然科学基金
【CateGory Index】: O657.32
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