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- W2235698522 abstract "Electrophoretic analysis of the water soluble fraction of chick lens fiber cells, the urea-soluble fraction, and the urea-insoluble plasma membrane fraction was performed in 5.13% polyacrylamide gels containing 1% sodium dodecyl sulfate (SDS). Five polypeptides were identified for the water soluble fraction. One polypeptide of molecular weight 22,500 daltons corresponded to subunits of α-crystallin, three polypeptides of molecular weights 25,000 daltons, 27,500 daltons, and 37,000 daltons corresponded to subunits of β-crystallins, and one polypeptide of 43,000 daltons corresponded to subunits of δ-crystallin. The water insoluble fraction contained twelve additional polypeptides with molecular weights ranging from 41,000 to 200,000 daltons. The 8 M urea soluble fraction (albuminoid) contained the 5 crystallin polypeptides as well as 8 additional bands. The major component of albuminoid consisted of a polypeptide of 41,000 daltons not found in the water soluble fraction of the lens. The urea-insoluble fraction (cell membranes) consisted of only 8 bands, one of which corresponded in molecular size with subunits of δ-crystallin and 2 with subunits of β-crystallin. However, the presence of lipid in the major membrane component (54.0%; with a mobility of a β-crystallin subunit) suggests that this component ist not a β-crystallin polypeptide." @default.
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- W2235698522 date "1976-01-01" @default.
- W2235698522 modified "2023-09-24" @default.
- W2235698522 title "The Protein Structure of Chick Lens Fiber Cell Membranes and Intracellular Matrix" @default.
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