Subunit Components in Salt-soluble and Insoluble Fractions of Carp Myofibrils during Frozen Storage

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  • Subunit Components in Salt-soluble and

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The changes of subunit components in salt (0.6M KCl)-soluble and salt-insolublfractions of carp myofibrils during frozen storage were followed by 7.5% polyacrylamide gel electrophoresis. Myofibrillar samples were suspended in 0.1M KCl solution containing 5 and 20mM Tris-maleate buffer (pH 7.2), and in 0.1M KCl solution without a buffer. Prepared samples were stored at three different temperatures: -4, -11, and-26°C. When the solubility decreased after 2-3 weeks at-4 and-11°C, the main components of the myofibrils in the salt-soluble fraction decreasedand weredetectable in the saltinsoluble fraction. The decrease of salt-solubleprotein at-11°C was larger than that observed at -4°C. At -4°C storage, theextentofthe decrease in the salt-soluble fraction and consequently that of the increasein the salt-insoluble fraction was relatively larger in the actin (A) component than in the myosin heavy chain (HC) component. At -11°C storage, the shift of HC component from the salt-soluble fraction to the salt-insoluble fraction on the last day of storage was larger than that of the A component in three Tris concentrations. As for the salt-insoluble fraction, the aggregated proteins which could not migrate into 7.5% polyacrylamide gel (>G component) was foundto be largerin th model system without the buffer than in that containing the buffer at any storage temperature. It seems that the formation of the >G component at-11 and-26°C without buffer accompanied the HC component.

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