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作 者:李津婴[1] 赵法[2] 郭俊生[2] 叶煦亭[3] 胡小健[4] 张志鸿[4] 周汉清[4]
机构地区:[1]第二军医大学长海医院,上海200433 [2]第二军医大学军队卫生教研室 [3]第二军医大学电镜室 [4]复旦大学生物物理系
出 处:《生物化学与生物物理进展》1997年第4期339-343,共5页Progress In Biochemistry and Biophysics
基 金:国家自然科学基金资助项目! (392 70 5 89)
摘 要:根据带 3蛋白 (阴离子交换蛋白 )拓扑学模式、氨基酸保守片段、功能片段、天然抗原表位 ,设计大鼠带 3膜外侧片段合成肽 ,制备抗合成肽 ( 1 2肽 )抗体 ,同时制备抗大片段带 3抗体加以印证 .多项免疫学实验鉴定结果表明 ,该 1 2肽是带 3抗原决定簇之一 ,也是带 3发挥阴离子转运功能的关键肽段 ;1 2肽的氨基酸组成与序列在各种属间高度保守 .免疫金银显色———扫描电镜结果给出该 1 2肽为带 3蛋白膜外侧区片段的最直接证据 .制备的抗带 3抗体可作为研究带 3结构与功能、探讨与带Based on the conservative sequences, topological, biochemical, physiological and immunological data of anion exchanger (AE, band 3 protein) families, a peptide included 12 amino acids (position 476~487: SKLIKIFQDYPL) was synthesized and the antibodies against this peptide and the native segment of band 3 from rat erythrocyte membrane were prepared. The findings of immunoblotting and anion transport studies indicated that the peptide is an essential segment of the anion transport which is a conservative sequence in mammals (rat, mouse as well as human). Immunoscanning electron microscopic study proved directly that the peptide is located at the peripheral domain of band 3 in rat erythrocyte membrane. The antibodies against band 3 are useful tools in studying the structures and functions of the anion transport protein and investigating the relationship between band 3 and diseases.
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