大鼠心脏蛋白质的二维电泳数据库。

A two-dimensional electrophoresis database of rat heart proteins.

作者信息

Li X P, Pleissner K P, Scheler C, Regitz-Zagrosek V, Salnikow J, Jungblut P R

机构信息

Max Volmer Institute of Biophysical Chemistry and Biochemistry, Technical University Berlin, Germany.

出版信息

Electrophoresis. 1999 Apr-May;20(4-5):891-7. doi: 10.1002/(SICI)1522-2683(19990101)20:4/5<891::AID-ELPS891>3.0.CO;2-2.

DOI:10.1002/(SICI)1522-2683(19990101)20:4/5<891::AID-ELPS891>3.0.CO;2-2

PMID:10344264

Abstract

More than 3000 myocardial protein species of Wistar Kyoto rat, an important animal model, were separated by high-resolution two-dimensional gel electrophoresis (2-DE) and characterized in terms of isoelectric point (pI) and molecular mass (Mr). Currently, the 2-DE database contains 64 identified proteins; forty-three were identified by peptide mass fingerprinting (PMF) using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), nine by exclusive comparison with other 2-DE heart protein databases, and in only 12 cases of 60 attempts N-terminal sequencing was successful. We used the Make2ddb software package downloaded from the ExPASy server for the construction of a rat myocardial 2-DE database. The Make2ddb package simplifies the creation of a new 2-DE database if the Melanie II software and a Sun workstation under Solaris are available. Our 2-DE database of rat heart proteins can be accessed at URL http://gelmatching.inf.fu-berlin.de/pleiss/2d.

摘要

通过高分辨率二维凝胶电泳（2-DE）分离了重要动物模型Wistar Kyoto大鼠的3000多种心肌蛋白，并根据等电点（pI）和分子量（Mr）对其进行了表征。目前，2-DE数据库包含64种已鉴定的蛋白质；43种通过使用基质辅助激光解吸/电离质谱（MALDI-MS）的肽质量指纹图谱（PMF）鉴定，9种通过与其他2-DE心脏蛋白质数据库进行独家比较鉴定，在60次尝试中只有12例N端测序成功。我们使用从ExPASy服务器下载的Make2ddb软件包构建大鼠心肌2-DE数据库。如果有Melanie II软件和Solaris下的Sun工作站，Make2ddb软件包可以简化新2-DE数据库的创建。我们的大鼠心脏蛋白质2-DE数据库可通过以下网址访问：http://gelmatching.inf.fu-berlin.de/pleiss/2d 。