Subject(s)
Cell Adhesion Molecules/isolation & purification , Cell Adhesion Molecules/metabolism , Phosphoproteins/isolation & purification , Phosphoproteins/metabolism , Animals , Baculoviridae/genetics , Blood Platelets/chemistry , Blood Platelets/metabolism , Blood Proteins/isolation & purification , Blood Proteins/metabolism , Cell Adhesion Molecules/blood , Cell Line , Chromatography, Affinity , Humans , Insecta , Microfilament Proteins/blood , Microfilament Proteins/isolation & purification , Microfilament Proteins/metabolism , Molecular Probes , Phosphoproteins/blood , Phosphorylation , Protein Binding , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Swine/bloodABSTRACT
Antibodies were raised against homogeneous preparations of component C of the methylreductase system from Methanococcus voltae and Methanobacterium thermoautotrophicum. Cells of these organisms were fixed with paraformaldehyde and/or glutaraldehyde, sectioned, and labeled with antibodies and colloidal gold-labeled protein A. In M. voltae the gold particles were predominantly located in the vicinity of the cytoplasmic membrane. In rare cases a similar result was obtained also with M. thermoautotrophicum. However, in all but a few of the ultrathin sections of this bacterium, the label was randomly distributed in the cell interior. If one assumes a reliable fixation of all cell components, these results would suggest that the two distantly related methanogens studied have distinctive patterns for the localization of component C. The results with M. voltae are in agreement with recent findings that the methylreductase system is involved in the generation of a proton-motive force at the membrane.