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Accession number;04A0022346
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| Title;Comparative Biochemical Characterization of Protease Systems Involving in Postmortem Tenderization of Avian Meats |
| Author;
MURAMOTO KOJI
(Graduate School of Life Sci., Tohoku Univ., JPN)
NAUDE R J
(Univ. Port Elizabeth)
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Journal Title;Shokuniku ni kansuru Josei Kenkyu Chosa Seika Hokokusho
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Journal Code:X0296A
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ISSN:
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VOL.21;NO.;PAGE.182-184(2003)
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| Figure&Table&Reference;TBL.4, REF.2 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Calcium-activated neutral proteinases(calpains) and their endogenous specific inhibitor calpastatin are present in a wide variety of tissues. Calpains are cysteine proteases that have an absolute requirement for Ca2+ for activity, and are heterodimers consisting of catalytic subunits of approximately 80kDa and regulatory subunits of 30kDa. Calpains have been shown to hydrolyze a wide variety of protein substrates. Although calpains could be involved in postmortem tenderization of meats, very little attention has been given to avian species. m- and .MU.-Calpain and calpastatin were purified and characterized from ostrich in this study. The proteases have molecular masses of 84k and 84k by SDS-PAGE, respectively. The pH and temperature optima were found to be 7.5 and 37.DEG.C. for the both. The calpain proteolytic system consists of at least three components: (1) the form of the proteinase that is fully active at micromolar concentrations of calcium; (2) the form of the proteinase that is fully active at millimolar concentrations of calcium; and (3) calpastatin, which inhibits the activity of both m- and .MU.-calpain at their respective calcium requirements. Ostrich calpastatin has a molecular mass of 323k and a pI of 4.7. (author abst.) |
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