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Electrophoretic studies of muscle proteins. II. Complex formation between delta protein, myogen and myosin

1971; Wiley; Volume: 77; Issue: 3 Linguagem: Inglês

10.1002/jcp.1040770302

1097-4652

W Amberson, Adelia C. Bauer,

thermodynamics and calorimetric analyses

Abstract In actin‐free extracts of rabbit white muscles complexes form between delta protein, myogen (mainly glycolytic enzymes) and myosin, detectable in electrophoretic patterns of both limbs. The complexes are concentration sensitive, nearly absent when total protein is below 5 mgm/ml, but increasing at higher concentrations. At 65 mgm/ml about 60% is bound at 1°C. Complex concentrations can be calculated by making Rayleigh fringe counts on two portions of the same solution, one more concentrated, the other diluted with buffer. A “fringe balance” can then be constructed which measures the forward movement, in the concentrated descending pattern, of those portions of myogen and myosin which have united with delta and moved with it in a fast position. Similar calculations are possible for the ascending limb. When commercial aldolase or lactic dehydrogenase solutions are mixed with concentrated extracts from which most free myogen has been removed the patterns show that portions of the added enzymes have complexed with myosin and delta and move with them in fast positions. Mixtures of pure aldolase and nearly pure myosin solutions also show com‐plexing, less well developed than when other enzymes are present. The glycolytic enzymes may have to unite with each other before they can readily complex with myosin and delta. There may be a lineal order of the glycolytic enzymes laid out along the fibrous proteins, permitting a rapid handling of their substrates.