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- W2118095938 abstract "Purified myofibrils were prepared from infraspinatus (tender) and rhomboideus (tough) muscles at 7 days postmortem and examined for myofibrillar/cytoskeleta1 protein degradation by using sodium dodecyl sulfate polyactylamide gel electrophoresis (SDS-PAGE). Four acrylamide/bisacrylamide ratios (37:1, 50:1, 75:l and 100:1) and two SDS-PAGE gel buffers (Tris-HCl, pH 8.0 and 8.9) were used to determine the optimum conditions for detection of titin and nebulin. Titin was degraded to a greater extent in myofibrils from the infraspinatus than in myofibrils from the rhomboideus. Very little nebulin was detected in either muscle. Use of acrylamide/bisacrylamide ratio of 37:1 and a gel buffer of pH 8.0 provided the most optimum conditions for detecting differences in the resolution of titin, nebulin and their apparent degradation products." @default.
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- W2118095938 date "1987-03-01" @default.
- W2118095938 modified "2023-09-27" @default.
- W2118095938 title "SDS-PAGE Conditions for Detection of Titin and Nebulin in Tender and Tough Bovine Muscles" @default.
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- W2118095938 doi "https://doi.org/10.1111/j.1365-2621.1987.tb06659.x" @default.
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