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Food Science

1995

Muscle biology

Articles 1 - 2 of 2

Full-Text Articles in Life Sciences

Myofibrillar Protein Degradation Patterns And Structural Changes In Skeletal Muscle From Electrically Stimulated Bos Taurus And Bos Indicus Crossbred Cattle , Chiung-Ying Ho Jan 1995

Myofibrillar Protein Degradation Patterns And Structural Changes In Skeletal Muscle From Electrically Stimulated Bos Taurus And Bos Indicus Crossbred Cattle , Chiung-Ying Ho

Retrospective Theses and Dissertations

Degradation of titin, nebulin, desmin and troponin-T, structural changes in nonstimulated (NS) and electrically stimulated (ES) bovine skeletal muscle and comparison of these changes in Angus x Jersey (AxJ) cattle (Bos taurus cross) with the changes in Brahman x Simmental (BxS) cattle (Bos indicus cross) were determined. Myofibrils for SDS-PAGE and Western blots and intact muscle samples for transmission electron microscopy were prepared at 0, 1, 3, 7, 14 and 28 days postmortem (PM). In SDS-PAGE, ES slightly accelerated the degradation of intact titin (T1 band), nebulin, desmin and troponin-T in AxJ samples. In Western blots of AxJ samples, ES ...


The Relationship Between The Calpain Enzyme System And The Postmortem Degradation Of Selected Myofibrillar Proteins , Elisabeth Jane Huff Lonergan Jan 1995

The Relationship Between The Calpain Enzyme System And The Postmortem Degradation Of Selected Myofibrillar Proteins , Elisabeth Jane Huff Lonergan

Retrospective Theses and Dissertations

The protease [mu]-calpain degrades the myofibrillar proteins titin, nebulin, filamin, desmin and troponin-T. Titin and nebulin have been reported to be affected by sample preparation. This study showed that there was little difference in the rate of degradation of the intact forms due to sample preparation (whole muscle preparations vs. purified myofibrils). The postmortem degradation of titin, nebulin, filamin, desmin, and troponin-T was monitored using SDS-PAGE and Western blotting techniques at 0, 1, 3, 7, 14, 28, and 56 days postmortem. Postmortem aged samples with lower shear force values exhibited faster degradation of the five myofibrillar proteins. Similar degradation ...