铁螯合物引起的蛋白质特异性切断  

Iron Chelate-Induced Specific Cleavage of Protein

作　　者：王宗睦[1] 高健[1] 丁跃梅 厉廷有[1] 

机构地区：[1]吉林大学分子生物学系,上海科技大学

出　　处：《吉林大学自然科学学报》1995年第3期106-108,共3页Acta Scientiarum Naturalium Universitatis Jilinensis

基　　金：国家自然科学基金

摘　　要：利用１－（Ｎ－溴乙酰－对氨基苄基）－ＥＤＴＡ，借助活泼溴的高离核性，对琉基。枯草杆菌蛋白酶的巯基亲核取代，进行化学偶联。将ＥＤＴＡ基团与Ｆｅ￣２＋螯合，在ｐＨ７．０，２５℃下用Ｈ＿２Ｏ＿２及抗坏血酸钠处理，使巯基－枯草杆菌蛋白酶的多肽链于Ｖａｌ￣８８－Ｓｅｒ￣８９处被特异地切断为两段。The conversion of Ser￣221 in subtilisin Carlsberg to Cys was carried out using the method pro- posed by Polgar et al.The Cys￣221 of obtained mercapto enzyme was alkylated with l-[p-(bromoac- etamido)benzyl] -EDTA and the resulted enzyme was treated with a solution containing H_2O_2,Fe￣2+and ascorbate at pH 7 and 25 ℃. It was found that the enzyme molecule was cleavaged specifically andthe only cleavaged site was at Val￣88 -Ser￣89 bond.

关 键 词：铁螯合物 特异性切断 枯草杆菌蛋白酶 蛋白质 

分 类 号：Q51[生物学—生物化学]