Nejvíce citovaný článek - PubMed ID 4977833
Regulation of the formation of protease in Bacillus megaterium. 3. Enzyme production under limitation of nitrogen source
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.
- MeSH
- Bacillus megaterium enzymologie genetika MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- endopeptidasy analýza MeSH
- gelová chromatografie MeSH
- mutace MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- endopeptidasy MeSH
A strain of Pseudomonas aeruginosa from soil produced large quantities of extracellular neutral proteinase and could utilize several organic substances as carbon and nitrogen sources for enzyme production. The growth media required the presence of a high amount of phosphate when glucose was the carbon source. The intermediates of citric-acid cycle acids supported the proteinase production more than any other carbon sources. However, complex nitrogenous substances supported enzyme production more efficiently. Higher concentration of casamino acids suppressed the protinase synthesis.
- MeSH
- alkoholy farmakologie MeSH
- aminokyseliny farmakologie MeSH
- dusík farmakologie MeSH
- endopeptidasy metabolismus MeSH
- glukosa farmakologie MeSH
- koncentrace vodíkových iontů MeSH
- kyseliny farmakologie MeSH
- peptony farmakologie MeSH
- Pseudomonas aeruginosa enzymologie MeSH
- uhlík farmakologie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- alkoholy MeSH
- aminokyseliny MeSH
- casamino acids MeSH Prohlížeč
- dusík MeSH
- endopeptidasy MeSH
- glukosa MeSH
- kyseliny MeSH
- peptony MeSH
- uhlík MeSH
- MeSH
- autoradiografie MeSH
- Bacillus megaterium růst a vývoj metabolismus MeSH
- Bacillus subtilis enzymologie MeSH
- bakteriální proteiny biosyntéza metabolismus MeSH
- bakteriologické techniky MeSH
- chlorid amonný metabolismus MeSH
- dusík metabolismus MeSH
- elektronová mikroskopie MeSH
- izotopy uhlíku MeSH
- kultivační média MeSH
- leucin metabolismus MeSH
- proteasy biosyntéza MeSH
- spory bakteriální růst a vývoj MeSH
- tritium MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- chlorid amonný MeSH
- dusík MeSH
- izotopy uhlíku MeSH
- kultivační média MeSH
- leucin MeSH
- proteasy MeSH
- tritium MeSH
- MeSH
- aminokyseliny farmakologie MeSH
- Bacillus megaterium účinky léků enzymologie růst a vývoj MeSH
- časové faktory MeSH
- cystein farmakologie MeSH
- enzymová indukce MeSH
- enzymová represe MeSH
- glukosa farmakologie MeSH
- izotopy uhlíku MeSH
- kultivační média MeSH
- peptony MeSH
- proteasy biosyntéza MeSH
- spektrofotometrie MeSH
- spory růst a vývoj MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- aminokyseliny MeSH
- cystein MeSH
- glukosa MeSH
- izotopy uhlíku MeSH
- kultivační média MeSH
- peptony MeSH
- proteasy MeSH