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- W1998881296 abstract "Abstract Gel chromatography on agarose of extracts from cortex and nucleus of the rabbit lens revealed considerable differences in the amounts of α- and high-molecular weight crystallin. Alpha-crystallin, high-molecular weight crystallin and urea-soluble fraction were compared using sodium dodecyl sulphate gel electrophoresis and isoelectric focusing in 6 m -urea. The cortical fractions revealed similar subunit structures. The same holds for the nuclear fractions. However, the subunit structures of the cortex and nucleus fractions differed greatly. On isoelectric focusing nuclear α-crystallin showed 12–13, cortical α-crystallin 4 polypeptide chains. Applying sodium dodecyl sulphate gel electrophoresis in the presence of dithiothreitol, cortical α-crystallin revealed two bands, nuclear α-crystallin three main bands and four minor bands. Two of the latter bands correspond with those of β-crystallins. In urea-soluble fractions of cortex and nucleus three additional bands corresponding with polypeptide chains with molecular weights between 52 000 and 65 000 Daltons were obtained. Cortical urea-insoluble fraction showed one single band with a molecular weight of 31 000 Daltons, whereas the nuclear urea-insoluble fraction revealed four additional minor bands with molecular weights ranging from 19 000–60 000 Daltons. Possible relationships between α-crystallin, high-molecular weight crystallin and urea-soluble fraction with respect to the insolubilization of lens proteins are discussed." @default.
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- W1998881296 date "1974-12-01" @default.
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- W1998881296 title "HM-crystallin as an intermediate in the conversion of water-soluble into water-insoluble rabbit lens proteins" @default.
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- W1998881296 doi "https://doi.org/10.1016/0014-4835(74)90092-x" @default.
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