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One of the low molecular weight proteins of bovine lens extract, designated as βs-crystallin, was purified by gel-filtration on Sephadex G-75 and chromatography on DEAE-Sephadex. The isolated protein appeared to be homogeneous as judged by gel-electrophoresis and ultracentrifugal analyses. The molar extinction coefficient at 278 mμ is 5·28 × 104. The N-terminal amino acid did not react with 2,4-dinitrofluorobenzene. There is evidence that the carboxyl-terminal group is glutamic acid. Amino acid analysis was performed with a recovery of 100·9% of the dry weight of the protein. The molecular weight, calculated from the amino acid composition is 28,402 and is consistent with the value determined by the approach-to-equilibrium method. The protein contains 246 amino acid residues with the following composition: Asp22 Thr7 Ser15 Glu31...
Four low molecular weight proteins, designated as β2-, γ0-, γ1- and γ2-crystallin, have been isolated from the cortex of bovine lenses by gel filtration on Sephadex G-75, followed by chromatography on DEAE-Sephadex. The isolated proteins were found to be homogeneous in starch gel and/or agar electrophoresis. Efforts to determine any amino terminal group in β2-crystallin with the use of 2, 4-dinitrofluorobenzene failed. The carboxyl-terminal group determinations of β2-crystallin yielded glutamic acid in submolar quantities. The amino acid composition of each of the four proteins was determined and the molecular weights were calculated from these findings. On the basis of the amino acid composition the isolated proteins could be divided into three groups, which differ widely in some amino acids. Some unique features of amino acid compos...
1. 1. The conformation in solution of eye-lens proteins obtained from cortical extracts of adult bovine lenses, was studied by means of the optical rotatory dispersion method. 2. 2. The rotatory data were analysed according to the modified two-term Drude equation, the Moffitt-Yang equation and the one-term Drude equation. 3. 3. The lens proteins appeared to consist of a mixture of α-helix, random coil and some other structure, which disappeared upon denaturation by acid, alkali or 8 M urea, and also in 2-chloroethanol. 4. 4. From a comparison with other proteins it seems probable that this other structure has a β conformation.
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