Intracellular proteolytic activities of B. megaterium KM occur soluble in the cytoplasm and periplasm and insoluble in the membrane. Two proteolytic enzymes were found in the cytoplasmic fraction by gel filtration on Sephadex G 150 and by polyacrylamide gel electrophoresis. The first enzyme called CI was stable, had a relative molecular mass of Mr = 105,000 (M = 105 kg/mol) and was inhibited by EDTA and PMSF, whereas the second, designated CII, was labile and had a relative molecular mass of Mr = 46,000 (M = 46 kg/mol). Because of its lability it could not be characterized in detail. In the "periplasm" only a single proteolytic enzyme P (Mr = 28,000; M = 28 kg/mol) inhibited by EDTA could be demonstrated. The extracellular enzyme exhibited similar properties. The membrane proteolytic activity was sensitive to PMSF and EDTA. The membrane enzymes have not yet been solubilized. In cells of the mutant KM 12 that does not produce the extracellular proteinase, only one type of proteinase, in all its properties identical with the cytoplasmic proteinase CI, could be demonstrated.

Institute of Microbiology Czechoslovak Academy of Sciences Prague

See more in PubMed

Folia Microbiol (Praha). 1966;11(2):82-8 PubMed

Folia Microbiol (Praha). 1984;29(4):273-81 PubMed

Bacteriol Rev. 1977 Sep;41(3):711-53 PubMed

Folia Microbiol (Praha). 1975;20(4):277-88 PubMed

Folia Microbiol (Praha). 1972;17(4):281-90 PubMed

J Bacteriol. 1988 Jan;170(1):136-40 PubMed

C R Acad Sci Hebd Seances Acad Sci D. 1971 Mar 29;272(13):1806-9 PubMed

Biochimie. 1979;61(3):385-91 PubMed

J Bacteriol. 1971 Sep;107(3):815-23 PubMed

Biochem Biophys Res Commun. 1972 Oct 17;49(2):328-34 PubMed

Folia Microbiol (Praha). 1969;14(1):70-6 PubMed

Biochem Biophys Res Commun. 1977 Jul 11;77(1):298-305 PubMed

Arch Microbiol. 1981 May;129(3):227-32 PubMed

Folia Microbiol (Praha). 1972;17(2):132-42 PubMed

J Bacteriol. 1983 Jan;153(1):511-9 PubMed

J Bacteriol. 1980 Feb;141(2):493-501 PubMed