硒蛋白P同功型突变体短肽hSelP82m分析  

Preparation and analysis of human selenoprotein Pmutant peptide hSel P82m

作　　者：王青[1] 窦科峰[1] 钱海利[2] 马庆久[3] 鲁建国[3] 宁力[3] 房青[2] 林晨[2] 

机构地区：[1]第四军医大学西京医院肝胆外科,陕西西安710033 [2]中国医学科学院中国协和医科大学肿瘤研究所分子肿瘤学国家重点实验室,北京100021 [3]第四军医大学唐都医院普通外科,陕西西安710038

出　　处：《第四军医大学学报》2005年第10期872-874,共3页Journal of the Fourth Military Medical University

基　　金：国家自然科学基金(30370302)

摘　　要：目的: 切割硒蛋白P同功型突变体活性肽hSelP137m,以得到可能具备相同生物学活性而氨基酸数目更少的短肽.方法: 利用生物信息学技术分析hSelP280m,hSelP137m的活性功能域,用羟胺切割hSelP137m,并用SDSPAGE及蛋白质印迹加以分析验证.结果: 切割hSelP137m后得到了82(28aa- 109aa)个氨基酸的多肽,在特定的位置出现了预期的目的蛋白条带.利用生物信息学技术加以分析,认为hSelP82m基本具备hSelP137m的生物学活性.结论: 经切割硒蛋白P同功型突变体活性肽hSelP137m,成功得到82个氨基酸的短肽hSelP82m,并且认为其基本具备hSelP137m的生物学活性.AIM: To obtain the potentially active shorter form of peptide with hSel P137m activity by chemically splitting SelP peptide mutant isoform.METHODS: The potential active domains of mutant hSel P280m and hSel P137m were analyzed by bioinformatics.hSel P137m was split by hydroxylamine and the result was analyzed by SDS-PAGE and Western blotting.RESULTS: The SDS-PAGE showed that hSel P137m was chemically split at the expected position between 28aa and 109aa.The split was also confirmed by Western blotting with polyclonal anti-hSel P137 antibody.Bioinformatics indicated that the hSel P82m fragment had similar biological activity to that of hSel P137m.CONCLUSION: The fragment hSel P82m has been obtained by cutting hSel P137m.Bioinformatical analysis indicates that the hSel P82m fragment has similar biological activity to that of hSel P137m.

关 键 词：硒 蛋白质类 肽类 计算生物学 化学裂解 印迹法 蛋白质 

分 类 号：Q71[生物学—分子生物学]