THE ALTERATION OF ENDOTOXIN BY POSTHEPARIN PLASMA AND ITS PURIFIED FRACTIONS. 2. RELATIONSHIP OF THE ENDOTOXIN DETOXIFYING ACTIVITY OF EUGLOBULIN FROM POSTHEPARIN PLASMA TO LIPOPROTEIN LIPASE
Abstract
Fractionation of the delipidized euglobulin from guinea pig postheparin plasma on DEAE-cellulose resulted in one protein peak in the effluent and two to three protein peaks following an NaCl-gradient. Both endotoxin detoxifying action and lipoprotein lipase activity were found in the fractions prior to the application of the NaCl-gradient, if the fractions were collected in heparin. Without added heparin, neither of the two activities was obtained. Associated with both detoxifying and lipase activities was the release of unesterified fatty acids and the endotoxin-clearing reaction. Heating the postheparin plasma euglobulin fraction either had no effect or partially inactivated the endotoxin-detoxifying factor, but destroyed lipoprotein lipase activity. Both unesterified fatty acid release from the endotoxin-albumin-euglobulin mixtures and the endotoxin-clearing reaction were destroyed by heat.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 29, 1966
- Accession Number
- AD0652075
Entities
People
- Duane R. Schultz
- Elmer L. Becker
Organizations
- Walter Reed Army Institute of Research