Subunit sizes of muscle proteins, as determined by sodium dodecyl sulphate gel electrophoresis

摘要: Abstract 1. Purified muscle proteins have been run on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The molecular sizes their subunits were determined by comparison with marker proteins. 2. Myofibrils dissolved sulphate, and separated into constituent electrophoresis. main components spectrum obtained identified, determined. In addition there was indication a protein subunit size 105 000 weight which has not previously described. 3. Sarcoplasmic glycolytic enzymes also studied. Only two these (phosphofructokinase phosphoglucose isomerase) gave this system significantly different from accepted values, both cases new values are nearly 20% lower. It is clear whether behave anomalously sulphate electrophoresis, or more conventional techniques for determining error.