Identification of mouse crystallins in 2D protein patterns by sequencing and mass spectrometry.: Application to cataract mutants
Identification of mouse crystallins in 2D protein patterns by sequencing and mass spectrometry.: Application to cataract mutants
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DOI：
10.1016/s0014-5793(98)01053-9
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发表时间：
1998-09-18
期刊：
影响因子：
3.5
通讯作者：
Klose, J
中科院分区：
文献类型：
--
作者：
Jungblut, PR;Otto, A;Klose, J
小鼠眼透镜蛋白质在大凝胶中通过双向电泳分离成1940个多肽斑点。通过蛋白质测序和质谱法鉴定了哺乳动物中普遍存在的所有16种晶体蛋白，除了（γ）-F，其显示与（γ）-E几乎相同的序列。两种晶体蛋白，（β）-A2和（γ）-S，首次显示在小鼠透镜中存在，对鼠白内障突变体Cat 2（nop）（（γ）-B基因）的研究表明，单基因突变可能影响广谱蛋白质，（C）1998年欧洲生物化学学会联合会。
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.