Studies on the Protein Moiety of Endotoxin from Gram-Negative Bacteria: Characterization of the Protein Moiety Isolated by Acetic Acid Hydrolysis of Endotoxin from S. marcescens 08
Abstract
'Conjugated' protein isolated from the endotoxin complex of Serratia marcescens 08 by 1% acetic acid hydrolysis was characterized by analytical ultracentrifugation, electrophoretic and immunological properties and chemical analysis. The chemical composition of 'conjugated' protein and other degraded fragments of endotoxin showed that all characteristic constituents of lipid A were present exclusively in 'conjugated' protein. Successive treatment of 'conjugated' protein with trypsin and pronase resulted in the isolation of corresponding tryptic and pronase cores which were characterized by an increased content of lipid A constituents. Lipid A was separated as an entity from the 'conjugated' protein only after hydrolysis with 0.1 N hydrochloric acid. 'Conjugated' protein and its tryptic and pronase cores were immunogenic and possessed a common antigenic determinant with 'simple' protein and its corresponding cores. Toxicity studies revealed that both 'conjugated' and 'simple' proteins retained to different degrees the toxic properties of whole endotoxin. Sodium dodecyl sulfate had an enhancing rather than diminishing effect on the toxicity of endotoxin and its various fragments.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 07, 1970
- Accession Number
- AD0716007
Entities
People
- P. Alaupovic
- W. Wober
Organizations
- University of Oklahoma