Calorimetric study of the interaction of lysozyme with aqueous 1-propanol.
Calorimetric study of the interaction of lysozyme with aqueous 1-propanol.
复制标题
溶菌酶与 1-丙醇水溶液相互作用的量热研究。
DOI：
10.1021/bi00514a016
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Velicelebi,G
中科院分区：
文献类型：
--
作者：
Sturtevant,JM;Velicelebi,G
蛋清溶菌酶(TV-乙酰尿素胺葡聚糖水解酶；EC 3.2。1.17)，从西格玛化学公司获得1级，3次结晶，透析，冷冻干燥的粉末。该产品在pH为4.0的0.05M甲酸铵缓冲液中溶解、透析，然后进行冷冻干燥。所有缓冲溶液均由分析级试剂配制而成。在脱气缓冲液中溶解冷冻干燥的蛋白质制备蛋白质溶液，在水溶液中用GB 2801%=26.5分光光度法测定其浓度(Bjuulf&Wadsó，1972)。吸光度测量是在10℃下进行的，根据DSC变性曲线判断，蛋白质在所有使用的酒精溶液中是天然的。所有的量热实验都是在0.04M甘氨酸缓冲液中进行的，该缓冲液在pH为2.0的ProH存在下调节为
Materials and MethodsHen egg white lysozyme (TV-acetylmuramide glycano-hydrolase; EC 3.2. 1.17) was obtained from Sigma Chemical Co. as grade 1, 3 times crystallized, dialyzed, and lyophilized powder. This product was further treated by dissolution in and dialysis against 0.05 M ammonium formate buffer at pH 4.0 and subsequent lyophilization. All buffer solutions were prepared from analytical grade reagents. Protein solutions were prepared by dissolving the lyophilized protein in degassed buffer, the concentrations being determined spectrophotometrically byusing£ 2801%= 26.5 in aqueous solution (Bjurulf & Wadsó, 1972). The absorbance measurements were carried out at 10 C where the protein was native in all the alcohol solutions employed as judged by DSC denaturation profiles. All the calorimetric experiments were carried out in 0.04 M glycine buffer adjusted in the presence of PrOH to pH 2.0 as