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Accession number;01A0468772
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| Title;Effect of Solvent Composition on the Precipitation of Cathepsin D Hydrolysates of .ALPHA.s1-Casein with Trichloroacetic Acid. |
| Author;
IGARASHI Y
(Hirosaki Univ., Aomori, Jpn)
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Journal Title;Milk Science
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Journal Code:F0966A
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ISSN:1343-0289
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VOL.50;NO.1;PAGE.17-23(2001)
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| Figure&Table&Reference;FIG.5, REF.17 |
| Pub. Country;Japan |
| Language;English |
| Abstract;Practically pure .ALPHA.s1-casein was separated from bovine skim milk by the precipitation procedure in 50% ethanol and urea solutions. It was hydrolysed by cathepsin D at 37.DEG.C. in 0.1 M sodium phosphate buffer (pH 6.0). A number of degradation products were observed by urea-polyacrylamide gel electrophoresis (PAGE) after the action of cathepsin D on .ALPHA.s1-casein but these components as well as undegraded .ALPHA.s1-casein were mostly precipitated by the addition of 2% (W/V) trichloroacetic acid (TCA). The addition of urea to the precipitation system partly released degradation products into the supernatant. In a precipitation system, 2% TCA-3.3 M urea, inclusion of ethylenediamine-tetraacetic acid (EDTA) up to 40 mM somewhat promoted precipitate formation. By adding Triton X-100 (0.1%) to the precipitation system, a considerable part of the components released into the supernatant. This increase in solubility was further promoted by the addition of both Triton X-100 and EDTA. These facts suggest that hydrophobic interactions between peptides including undegraded protein must be taken into account in performing fractionation of enzymatic degradation products of .ALPHA.s1-casein. (author abst.) |
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