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测得了长白山白眉蝮蛇毒精氨酸酯酶 1的最适反应的pH范围为 7.0～ 8.0 ,且与酶反应底物对甲苯磺酰-L -精氨酸甲酯 (TAME)的反应无明显的最适应反应温度 .荧光光谱的研究结果表明 :该酶的酪氨酸残基的荧光被色氨酸残基的荧光所掩盖 ;同步荧光光谱结果表明 :当发射波长与激发波长差Δλ分别为 2 0nm和 75nm时 ,精氨酸酯酶 1的荧光光谱分别由酪氨酸 (Tyr)和色氨酸 (Trp)残基所贡献 ,且处于亲水性环境中 ;精氨酸酯酶 1的荧光发射强度受溶液酸度变化的影响 .I- ,Acr和NBS对精氨酸酯酶 1的荧光淬灭结果表明这种酶中含有多个色氨酸残基 ,且处于不同的微环境中。
The optimum pH range of arginase esterase 1 in Changbai Mountain was 8.0 ~ 8.0, and the reaction with the enzyme reaction substrate tosyl - L - arginine methyl ester (TAME) showed no significant The most suitable reaction temperature.The results of fluorescence spectroscopy showed that the fluorescence of tyrosine residues of this enzyme was covered by the fluorescence of tryptophan residues.The results of synchronous fluorescence spectroscopy showed that when the difference between the emission wavelength and the excitation wavelength is 2λ Fluorescence spectra of arginase esterase 1 are contributed by tyrosine (Tyr) and tryptophan (Trp) residues, respectively, at 0 nm and 75 nm, and are in a hydrophilic environment; the fluorescence of arginase esterase 1 The emission intensity was affected by the change of acidity of the solution.The fluorescence quenching results of arginine esterase 1 by I-, Acr and NBS showed that this enzyme contained many tryptophan residues and was in different microenvironment.