Abstract:
:The molecular weight of the protein moiety of a phospholipoprotein complex isolated from Pseudomonas facilis has been examined with a variety of sodium dodecylsulfate-polyacrylamide gel electrophoretic systems. A molecular weight of 35 000 was determined for the protein in all analyses. A 35 000-dalton protein was present in the EDTA extract of P. facilis and in the cytoplasmic and outer membrane fractions, but not in the lipopolysaccharide and peptidoglycan. Prior inoculation of mice with the phospholipoprotein complex led to a 7.5- to 15-fold increase in the LD50 when mice were subsequently inoculated with Salmonella typhimurium; this pathogen has a cell-surface protein which cross-reacts immunologically with antibody to the P. facilis phospholipoprotein complex.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Jones RC,McFadden BAdoi
10.1007/BF00427842subject
Has Abstractpub_date
1977-10-24 00:00:00pages
37-43issue
1eissn
0302-8933issn
1432-072Xjournal_volume
115pub_type
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