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紫外差光谱是研究蛋白质在溶液中构象的有用工具,能揭示蛋白质中多种生色的氨基酸残基的存在和状态,并广泛用于多种酶类的必要基团、作用机理、过液态的存在等多方面的研究。前报I已证明,激活剂LIA能显著提高溶菌酶的活力,且是以无竞争的方式,随机地与溶菌酶结合的机理使其催化能力成倍地提高。显然,激活剂的加入使溶菌酶的结构,特别是在溶液中的空间构象发生了有利于催化作用的变化。为了弄清LIA诱导的溶菌酶构象的变化及在激活作用中所涉及的分子机理,我们进一步探索了溶菌酶与激活剂,底物相互作用的紫外差光谱。
UV spectrum is a useful tool to study the conformation of proteins in solution. It can reveal the existence and status of many chromophore amino acid residues in proteins and is widely used in essential groups, mechanism of action, over-liquid There are many other aspects of research. The previous report I has demonstrated that the activator LIA can significantly increase the activity of lysozyme and that its catalytic capacity is exponentially increased by a mechanism that is randomly combined with lysozyme in an uncontested manner. Obviously, the addition of activator makes the structure of lysozyme, especially the spatial conformation in solution, to favor the catalytic changes. In order to clarify the LIA-induced changes in the conformation of lysozyme and the molecular mechanism involved in the activation, we further explored the UV-spectrum of interaction between Lysozyme and activator and substrate.