Characterization of the chemical and physical properties of a novel B-lymphocyte activator, endotoxin protein.
Endotoxin protein, a novel mouse B-lymphocyte mitogen, is a hydrophobic acidic compound composed of approximately 85% protein and 2.2% glucosamine, but no 2-keto-3-deoxyoctonate. Endotoxin protein also contains lipid, and analysis of the fatty acids in this material demonstrated the presence of beta-hydroxymyristate, a marker for lipid A. In addition, analysis of endotoxin protein by polyacrylamide gel electrophoresis showed that it is heterogeneous, containing four or five major polypeptides, depending upon the bacterial species from which it was isolated. The mitogenicity of endotoxin protein was diminished by alkaline hydrolysis, but not by treatment with hydrochloric or acetic acid. Furthermore, its activity was resistant to digestion with trypsin, chymotrypsin, and pronase and was only partially degraded by papain.
D000818:Animals; D001402:B-Lymphocytes / Q000502:physiology*; D001426:Bacterial Proteins / Q000032:analysis* / Q000494:pharmacology; D004731:Endotoxins; D005227:Fatty Acids / Q000032:analysis; D006868:Hydrolysis; D008565:Membrane Proteins / Q000032:analysis* / Q000494:pharmacology; D051379:Mice; D008934:Mitogens / Q000032:analysis*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000494:pharmacology; D010455:Peptides / Q000032:analysis
D001426:Bacterial Proteins; D004731:Endotoxins; D005227:Fatty Acids; D008565:Membrane Proteins; D008934:Mitogens; D010455:Peptides; D010447:Peptide Hydrolases