Abstract
A streptomycete isolated from cow manure produces an extracellular enzyme capable of lysing the pseudomurein-containing methanogen Methanobacterium formicicum. The lytic activity has been partially purified from culture fluid and appears to be a serine protease. Similar lytic activity has been fractionated from pronase. Optimal conditions have been developed for lysis of M. formicicum by commercial preparations of proteinase K. The three lytic enzymes have been partially characterized. The results with the three enzyme preparations tend to confirm that proteolytic enzymes are capable of lysing methanogen cells.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference42 articles.
1. Adams M. H. 1959. Adsorption of phage to host cell p. 146. In Bacteriophages. Intersciences Publishers New York.
2. Methanogens: reevaluation of a unique biological group;Balch W. E.;Microbiol. Rev.,1979
3. Buchanan R. E. and N. E. Gibbons (ed.). 1974. Bergey's manual of determinative bacteriology 8th ed. The Williams & Wilkins Co. Baltimore.
4. Enzymic characterization of rabbit blastocyst proteinase with synthetic substrates of trypsinlike enzymes;Denker H.;Hoppe-Seyler's Z. Physiol. Chem,1979
5. Chemiosmotic coupling in Methanobacterium thermoautotropicum: hydrogen-dependent adenosine 5'- triphosphate synthesis by subcellular particles;Doddema H. J.;J. Bacteriol.,1979
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