Subunits of Alpha-Crystallin from Adult and Embryonic Cattle Lens
Subunits of Alpha-Crystallin from Adult and Embryonic Cattle Lens
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来自成年牛和胚胎牛晶状体的α-晶状体蛋白亚基
DOI：
10.1038/220790a0
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发表时间：
1968
期刊：
影响因子：
64.8
通讯作者：
H. Bloemendal
中科院分区：
文献类型：
--
作者：
J. Schoenmakers;H. Bloemendal
该透镜最近被用于研究体外 1-4 和器官培养 5 中的蛋白质生物合成。晶状体组织之所以有吸引力，是因为它是为数不多的哺乳动物系统之一，只能产生数量非常有限的特定蛋白质，例如晶状体蛋白。为了在体外或体内研究蛋白质生物合成，准确了解生物合成产物的性质是先决条件。之前的工作 6-8 为 α-晶状体蛋白的亚基结构提供了证据。在碱性 pH 值下，α-晶状体蛋白在含有 6 M 尿素的聚丙烯酰胺凝胶上的电泳图谱表明亚基存在相当大的异质性（图 1a）。另一方面，在酸性 pH 值（图 1b）或碱性 pH8 的 1% 十二烷基硫酸钠中只能观察到两条带。
THE lens has recently been used to study protein biosynthesis both in vitro1–4 and in organ culture5. Lens tissue is attractive because it is one of the few mammalian systems which manufacture only a very limited number of specific proteins, in casu the crystallins. In order to study protein biosynthesis in vitro or in vivo, exact knowledge of the nature of the biosynthetic product is a prerequisite. Previous work6–8 has provided evidence for a subunit structure of α-crystallin. The electrophoresis patterns of α-crystallin on polyacrylamide gel containing 6 M urea at alkaline pH suggest a considerable heterogeneity of the subunits (Fig. 1a). On the other hand, only two bands can be observed either at acid pH (Fig. 1b) or in 1 per cent sodium dodecylsulphate at alkaline pH8.