Abstract
1. 1. A method characterizing the fully active gramicidin S-synthetase (EC.6 6.3.2.−) multienzyme in protein mixtures by a combination of sedimentation and polyacrylamide gel electrophoretic mobility data has been described. 2. 2. The molecular weight of 280 000 has been reevaluated by gradient centrifugation, gel filtration, and polyacrylamide gel electrophoresis in presence of sodium dodecyl sulfate. The size of the multienzyme is not changed by sodium dodecyl sulfate treatment. 3. 3. In polyacrylamide gel electrophoresis dimerisation occurs in Tris, while two bands, which may represent monomer and dimer, are observed in phosphate. 4. 4. Reliability of molecular weight determinations of sodium dodecyl sulfate-protein complexes of sizes up to 300 000 daltons has been determined, correlating either mobilities or retardation coefficients.
Published Version
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