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Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39 |
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| Authors: | Jean-Marie Frère Ramon Moreno Jean-Marie Ghuysen Harold R Perkins Louis Dierickx and Lucien Delcambe |
| Institution: | Service de Microbiologie, Faculté de Médecine, Institut de Botanique, Université de Liège, Sart Tilman, 4000 Liège, Belgium;National Institute for Medical Research, Mill Hill, London NW7 1AA, U.K.;Centre National pour la Production et l''Etude de Substances d''Origine Microbienne, Boulevard de la Constitution, 32, 4000 Liège, Belgium |
| Abstract: | The exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase-transpeptidase from Streptomyces R61. |
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