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BAPBE的合成及其铁螯合物对蛋白质的切断作用
Synthesis of BAPBE and Cleavage of Proteins via Protein-BAPBE-Fe2+ Conjugates
【摘要】 设计、合成了一种新的蛋白质特异性氧化断裂试剂BAPBE,用它共价修饰BSA的唯一疏基.修饰物与Fe2+螯合,在pH7.0、25℃下用H2O2及抗坏血酸钠处理,使BSA发生2种方式的断裂,产生4种BSA片段,但在相同条件下巯基枯草杆菌蛋白酶未被切断.
【Abstract】 A new protein cleaving reagent, 1-[4-(4-bromoacetylamidophenoxy)benzyl]EDTA (BAPBE), was synthesized from tyrosin in 7 steps. Only the mercapto group of BSA was alkylated with BAPBE and then the resulted modification, BSA-BAPBE, was treated with a solution containing Fe2+ and H2O2/ascorbic acid successively. It was found that BSA was cleft specifically in four fragments, their Mw were 5.7×103, 3.6×103, 3.0×103 and ≤103 respectively. Under the same condition, however, the thiol-subtilisin-BAPBE conjugate was unaffected.
【关键词】 蛋白质;
特异性断裂;
1-[4-(N-溴乙酰-4-氨基苯氧基)苄基]-EDTA;
【Key words】 protein; specific cleavage; 1-[4(4-bromoacetyl-amidophenoxy)benzyl] EDTA (BAPBE);
【Key words】 protein; specific cleavage; 1-[4(4-bromoacetyl-amidophenoxy)benzyl] EDTA (BAPBE);
【基金】 国家自然科学基金
- 【文献出处】 吉林大学自然科学学报 ,ACTA SCIENTIARIUM NATURALIUM UNIVERSITATIS JILINENSIS , 编辑部邮箱 ,1997年04期
- 【分类号】O629.73
- 【下载频次】32