Abstract
Muscle proteins were labeled by incubating isolated frog sartorius muscles with [ 3H]- or [ 14C]phenylalanine. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of plasma membrane fractions revealed a major protein band with an apparent molecular weight of approx. 96 000. Radioactivity in this band showed a clearly delineated decrease, relative to other bands, when previously labeled muscles were induced to contract either by electrical stimulation or by increasing the influx of Ca 2+ from the incubation medium. It is postulated that a Ca 2+-activated neutral protease may account for this decrease in labeled membrane protein.
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