Abstract
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.
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SCHOENMAKERS, J., BLOEMENDAL, H. Subunits of Alpha-Crystallin from Adult and Embryonic Cattle Lens. Nature 220, 790–791 (1968). https://doi.org/10.1038/220790a0
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DOI: https://doi.org/10.1038/220790a0
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