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Immunochemistry and localization of the enzyme disaggregatase in Methanosarcina mazei
- Source :
- Journal of Bacteriology; May 1993, Vol. 175 Issue: 10 p3115-3120, 6p
- Publication Year :
- 1993
-
Abstract
- The enzyme disaggregatase (Dag) from Methanosarcina mazei was studied immunochemically. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of purified Dag under reducing and nonreducing conditions revealed a single band with a 94-kDa molecular mass. Dag was found to be immunogenic in rabbits; a polyclonal antibody probe was prepared and used to detect the enzyme by slide immunoenzymatic assay, immunofluorescence, and immunoblotting in various species of Methanosarcina known to convert from packets to single cells, including M. mazei. The enzyme could not be detected in other members of the family Methanosarcinaceae that do not convert. By immunogold electron microscopy, Dag was mapped to the cell wall of packets and to the cell membrane of single cells of two M. mazei strains.
Details
- Language :
- English
- ISSN :
- 00219193 and 10985530
- Volume :
- 175
- Issue :
- 10
- Database :
- Supplemental Index
- Journal :
- Journal of Bacteriology
- Publication Type :
- Periodical
- Accession number :
- ejs57627785
- Full Text :
- https://doi.org/10.1128/jb.175.10.3115-3120.1993