Electrophoretic separation of beta A4 peptides (1-40) and (1-42)

Electrophoretic separation of beta A4 peptides (1-40) and (1-42)
复制标题

DOI:
10.1006/abio.1996.0195
复制
发表时间:
1996-05-15
影响因子:
2.9
通讯作者:
Staufenbiel, M
Staufenbiel, M
中科院分区:
生物学4区
文献类型:
--
作者:
Klafki, HW;Wiltfang, J;Staufenbiel, M

文献摘要

被引文献

相似文献

比较了不同的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法(SDS-PAGE)对合成β-淀粉样多肽βA4(1-40)和βA4(1-42)的分离效果。在分离凝胶中加入8M尿素,并使用比星和硫酸盐分别作为拖带离子和前导离子的多相缓冲体系(比星/Tris/尿素凝胶),可以获得清晰的拆分。在这些条件下,较长的多肽迁移得比氨基酸40结束的要快。通过免疫沉淀和电泳分离转淀粉样前体蛋白cDNAs的细胞分泌的放射性标记多肽,证明了该系统在分析细胞代谢过程中产生的βA4相关多肽的有效性。(C)1996年学术出版社。
Different sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) systems designed for the separation of peptides were compared for their usefulness in separating synthetic beta-amyloid peptides beta A4 (1-40) and beta A4 (1-42). Clear resolution was achieved by addition of 8 M urea to the separation gel and use of a multiphasic buffer system employing bicine and sulfate as trailing and leading ions, respectively (bicine/Tris/urea gels). Under these conditions, the longer peptide migrated faster than the one ending at amino acid 40. The usefulness of this SDS-PAGE system for the analysis of beta A4-related peptides generated during cellular metabolism was demonstrated by immunoprecipitation and electrophoretic separation of radiolabeled peptides secreted by cells transfected with amyloid precursor protein cDNAs. (C) 1996 Academic Press, Inc.