Key result
An acrylamide/bisacrylamide ratio of 37:1 and a gel buffer of pH 8.0 provided the optimum conditions for detecting differences in the resolution of titin and nebulin in bovine muscles.
An acrylamide/bisacrylamide ratio of 37:1 and a gel buffer of pH 8.0 are optimal for detecting titin and nebulin degradation in bovine muscle using SDS-PAGE.
Optimizes titin/nebulin SDS-PAGE in bovine muscle; leaves open translation to human cardiac protein studies.
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.
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PATERSON et al. (1987) studied this question. SDS-PAGE conditions (acrylamide/bisacrylamide ratios and gel buffers) was evaluated on Optimum conditions for detection of titin and nebulin. An acrylamide/bisacrylamide ratio of 37:1 and a gel buffer of pH 8.0 provided the optimum conditions for detecting differences in the resolution of titin and nebulin in bovine muscles.
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