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研究了含内蛋白子的前体蛋白［麦芽糖结合蛋白－内蛋白子－几丁质酶结合区（ＭＹＢ）］在脲溶液中的分子构象及变性和复性过程中剪切活性与光谱变化的关系。结果表明，剪切活性随脲浓度的增加而逐渐丧失；当脲浓度大于６ｍｏｌ／Ｌ时，活性完全丧失。变性过程中Ａ２８０ｎｍ随变性程度增加而增强，复性后Ａ２８０ｎｍ与天然态Ａ２８０ｎｍ值相近，剪切活性随之恢复。说明构象松散先于剪切活性，可能在重折叠时，构象核化对剪切活性致关重要。
The molecular conformation and the changes of the shear activity and spectral changes during the denaturing and refolding of the precursor protein containing the endoprotein [maltose-binding protein-endoprotein-chitinase (MYB)] in urea solution relationship. The results showed that the shear activity gradually lost with the increase of urea concentration. When urea concentration was more than 6mol / L, the activity was completely lost. In the process of denaturation, A280nm increased with the degree of degeneration, and A280nm after refolding was similar to A280nm in natural state, and the shear activity recovered subsequently. It shows that the conformation loosely precedes the shear activity, and it may be that during the refolding, conformational nucleation is crucial to the shear activity.