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Characterization of enzymatic activity of lysozyme in lysozyme-ovotransferrin complex before and after treatment with trypsin

机译:对溶菌酶的酶活性和之前在lysozyme-ovotransferrin复杂治疗后用胰蛋白酶

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摘要

The native complex of lysozyme and ovotransferrin was isolated after the separation of egg white proteins using non-denaturing isoelectric focusing, and mobilization toward the cathode by replacement of the cathodic sodium hydroxide solution with a phosphoric acid solution. The treatment of the lysozyme-ovotransferrin complex with trypsin significantly increased the enzymatic activity of lysozyme. Likewise, an increase in the enzymatic activity of lysozyme was also obtained when a mixture of the purified lysozyme and ovotransferrin was treated with trypsin. The increase in lysozyme enzymatic activity after tryptic treatment of the lysozyme-ovotransferrin complex resulted from the liberation of lysozyme from this complex. This was a consequence of the resistance of lysozyme to tryptic digestion and the digestion of ovotransferrin by trypsin into peptide fragments, which do not bind the lysozyme. The developed methodology could be used for the separation and isolation of other protein complexes and for testing their enzymatic and other activities.
机译:溶菌酶和ovotransferrin本机复杂分离后的分离蛋白吗使用non-denaturing蛋白质等电点聚焦,动员向阴极更换阴极的氢氧化钠解决方案与磷酸的解决方案。lysozyme-ovotransferrin复杂的治疗用胰蛋白酶显著增加了溶菌酶的酶活性。溶菌酶的酶活性的增加也获得了纯化的混合物溶菌酶,ovotransferrin处理胰蛋白酶。活动后胰蛋白酶的治疗的lysozyme-ovotransferrin复杂的从这个复杂的解放的溶菌酶。溶菌酶的阻力的结果吗胰蛋白酶的消化和消化ovotransferrin通过胰蛋白酶为肽片段,不绑定的溶菌酶。方法可以用于分离和其他蛋白质复合物和隔离测试他们的酶和其他活动。

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