Extracellular proteases in Erwinia-chrysanthemi
1986
Wandersman , Cécile (Institut Pasteur de Paris, Paris(France). Unité de Génétique Moléculaire) | Andro , Thierry (Institut National de la Recherche Agronomique(France). UR 0217 Laboratoire de Pathologie végétale. VERS GRIGN PARIS PATHO V, Centre de recherche de Versailles-Grignon. Santé des Plantes et Environnement) | Bertheau , Yves (INRA (France). UR 0217 Laboratoire de Pathologie végétale)
Extracellular proteolytic enzyme activity has been detected in cultures of Erwinia chrysanthemi. This activity, which appears when the cells are grown in the presence of peptides, is rather unstable. A hyperproteolytic mutant was isolated which produces two proteases of apparent polypeptide molecular mass of 50 and 55 kDa, respectively. The 50 kDa protease, which is produced in the largest amounts, has been purified to near homogeneity. It has the properties of a neutral serine protease. The 50 and 55 kDa proteases are unrelated antigenically. Preliminary evidence suggests that both proteases are also produced by the wild-type strain, but that they are either produced in much smaller quantities or are much less stable.
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