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- W1982516351 abstract "1. Purified muscle proteins have been run on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The molecular sizes of their subunits were determined by comparison with marker proteins. 2. Myofibrils were dissolved in sodium dodecyl sulphate, and separated into the constituent subunits on electrophoresis. The main components of the spectrum obtained were identified, and their sizes determined. In addition there was indication of the presence of a protein of subunit size 105 000 molecular weight which has not previously been described. 3. Sarcoplasmic glycolytic enzymes were also studied. Only two of these (phosphofructokinase and phosphoglucose isomerase) gave subunit sizes in this system significantly different from accepted values, in both cases the new values are nearly 20% lower. It is not clear whether these proteins behave anomalously in dodecyl sulphate electrophoresis, or whether the more conventional techniques for determining molecular sizes are in error." @default.
- W1982516351 created "2016-06-24" @default.
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- W1982516351 date "1971-05-01" @default.
- W1982516351 modified "2023-09-27" @default.
- W1982516351 title "Subunit sizes of muscle proteins, as determined by sodium dodecyl sulphate gel electrophoresis" @default.
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- W1982516351 doi "https://doi.org/10.1016/0005-2795(71)90221-2" @default.
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