PHOSPHATIDYLSERINE-BOVINE SERUM ALBUMIN INTERACTIONS
Abstract
Highly purified preparations of phosphatidylserine and lecithin were obtained by the application of countercurrent distribution methods. It was demonstrated that a combination of these two components resulted in the formation of a highly active procoagulant substance. Turbidimetric methods were used to demonstrate that bovine serum albumin will bind phosphatidylserine. Removal of fatty acids from crystalline bovine serum albumin resulted in the appearance of a substance with sedimentation rate similar to that of the albumin dimer, S20,w = 6.41. Even though extraction of the lipid did not affect the -SH content of bovine serum albumin, the dimerization could be reversed by treatment with cysteine. This treatment resulted in a product which was free of lipid, with the same centrifugal and electrophoretic characteristics as native crystalline bovine serum albumin. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 20, 1961
- Accession Number
- AD0253651
Entities
People
- Donald G. Therriault
Organizations
- United States Army Medical Research Laboratory