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질트리코모나스에 존재하는 Azocasein 분해효소의 특성 분석
민득영,류재숙,손혁진,윤경봉 한양대학교 의과대학 1994 한양의대 학술지 Vol.14 No.1
The proteinases as potential histolytic and cytotoxic components of parasitic protozoa play the important role in the host-parasite relationship. Also the proteinase of T.vaginalis may expect to play the certain role in the host-parasite relationship during the infection, even though a few of the fundamental information is available. The present study was aimed to characterize the proteinase obtained from homogenates of T.vaginalis. Fractionation of T.vaginalis homogenates employing the sucrose density gradient and protein extraction using biological detergent was used as the enzyme source. Proteinase activity was assessed using azocasein(AZC) as substrate. Following the development of the optimal assay, the general properties of the enzyme have been examined with respect to pH dependence, effect of incubation temperature, incubation time, and effects of proteinase ingibitor and metal ions. The results were as follows: 1.AZCase of T.vaginalis showed the maximum enzyme activity at pH 6.0 with 100nM Phosphate buffer, andrevealed the partial enzyme activity at pH 3.5 with 100mM citrate buffer and at pH 8.5 with 100mM Tris-HCl buffer. 2.AZCase of T.vaginalis was heat-stable and showed the highest enzyme activity at 50℃. 3.The time course of AZCase revealed the linear proportionality for 4 hours. 4.AZCase of T.vaginalis had ingibitor sensitivity characteristic of cysteine proteinases. Leupeptin, antipain and chymostatin showed the complete inhibition of enzyme activity and these enzymes had partially ingibitor sensitivity of metallo-proteinases. 5.AZCase of T.vaginalis was stimulated by 20mM dithiothreitol(DTT) and 10mM cysteine. 6.AZCase of T.vaginalis was inhibited by Cu²,Hg² , Zn² ions in several divalent cations assayed. In conclusion, it is assumed that the AZCase of T.vaginalis is heat-stable, dithiothreitol(DTT)0dependent cysteinyl proteinase, and inhibited by Cu Hg², Zn² ions.
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