Identification of mouse crystallins in 2D protein patterns by sequencing and mass spectrometry.: Application to cataract mutants

被引：29

作者：

Jungblut, PR

Otto, A

Favor, J

Löwe, M

Müller, EC

Kastner, M

Sperling, K

Klose, J

机构：

[1] Humboldt Univ, Charite, Klinikum Rudolf Virchow, Inst Humangenet, D-13353 Berlin, Germany

[2] Max Planck Inst Infekt Biol, D-10117 Berlin, Germany

[3] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

[4] GSF, Forschungszentrum Neuherberg, Inst Saugetiergenet, D-85758 Oberschleissheim, Germany

[5] Free Univ Berlin, Klinikum Benjamin Franklin, Inst Klin Pharmakol, D-14195 Berlin, Germany

来源：

FEBS LETTERS | 1998年 / 435卷 / 2-3期

关键词：

mouse; eye lens; crystallin; cataract; two-dimensional electrophoresis; mass spectrometry;

D O I：

10.1016/S0014-5793(98)01053-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The eye lens proteins of the mouse were separated into 1940 polypeptide spots by two-dimensional electrophoresis in large gels. All 16 crystallins ubiquitous in mammals were identified by protein sequencing and mass spectrometry except for (gamma)-F, which shows an almost identical sequence with (gamma)-E, Two crystallins, (beta)-A2 and (gamma)-S, were shown for the first time to occur in the mouse lens, An investigation of the murine cataract mutant Cat2(nop) ((gamma)-B gene) demonstrated that a monogenic mutation might affect a broad spectrum of proteins, (C) 1998 Federation of European Biochemical Societies.

引用

页码：131 / 137

页数：7