Extracellular proteases in Erwinia-chrysanthemi
Résumé
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.
Domaines
Autre [q-bio.OT]
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1986_Wandersman_journal of general microbiology_1.pdf (1.06 Mo)
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