[en] The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G was purified to protein homogeneity and compared with the exocellular DD-carboxypeptidases-transpeptidases of Streptomyces R61 and Actinomadura R39. The S. albus G enzyme, as it is isolated, occurs in two forms. Enzyme I (30% of the total amount) and enzyme II (70% of the total amount) are identical in all respects, except that, by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate, enzyme I has an apparent mol. wt. (9000) that is half of that found by molecular-sieve filtration under non-denaturing conditions. Irrespective of the technique used, enzyme II has an apparent mol. wt. of about 18500.
Disciplines :
Microbiology
Author, co-author :
Duez, Colette ; Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Frère, Jean-Marie ; Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiolog
Geurts, Francine; Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiolog
Ghuysen, Jean-Marie ; Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiolog
Dierickx, Louis; Centre National pour la Production et l'Etude de Substances d'Origine Microbienne
Delcambe, Lucien; Centre National pour la Production et l'Etude de Substances d'Origine Microbienne
Language :
English
Title :
The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus Gl. Purification and chemical properties
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