title: Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens.
abstract: Xenorhabdus luminescens Hm cultured in gelatin broth produced a single extracellular protease. The protease was purified by a factor of 500 and characterized as a monomeric protein with an approximate molecular weight of 61,000. On the basis of inhibitor studies and its pH optimum, the protease was classified as an alkaline metalloprotease with a pH optimum near 8; the isoelectric point of the enzyme is 4.2 +/- 0.2. The protease may be a major factor in the ecology of X. luminescens, which is carried as a symbiom of some parasitic nematodes.
authors.affiliation: Center for Great Lakes Studies, University of Wisconsin-Milwaukee, 600 E. Greenfield Avenue, Milwaukee, Wisconsin 53204.
authors.forename: T M
authors.initials: TM
authors.lastname: Schmidt
authors.forename: B
authors.initials: B
authors.lastname: Bleakley
authors.forename: K H
authors.initials: KH
authors.lastname: Nealson