STUDIES ON THE PROPERTIES OF FIBRINOGEN-FREE LOW GLOBULIN PLASMA PROTEIN SOLUTIONS
Abstract
Cold ethanol water mixtures have been used to partially fractionate human plasma for the preparation of heat stable plasma protein solution. Ethanol concentrations ranging from 11 to 40% for the separation of the crude gamma globulin fraction have led to plasma protein mixtures in the supernatant fluid of varying electrophoretic concentrations of albumin; the higher the ethanol concentration, the higher the purity of albumin. When the dry powder was reconstituted to 5% protein with a mixture of 0.004M acetyl-DL-tryptophanate and 0.004M caprylate in water and heated for ten hours at 60 C., the albumin and beta globulins appeared to decrease and the alpha globulin to increase. In the ultracentrifuge all heated preparations contained a small amount of fast moving component. The ratio of the area of the main component of the heated solutions to that of the unheated was on the average 0.98. The amount of fast moving component in Fraction IV-1+IV-4+V decreased with increased ethanol concentration for Fraction II+III separation. An alpha-globulin normally precipitated in Fraction IV-4 of Cohn has been found to be the protein responsible for the fast moving ultracentrifuge component following 10 hours heating at 60 C. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 31, 1961
- Accession Number
- AD0262780
Entities
People
- Dwight J. Mulford
Organizations
- University of Kansas