Reconstitution of Rh (D) Antigen Activity from Human Erythrocyte Membranes Solubilized by Deoxycholate
- 4 April 1975
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 188 (4183) , 66-67
- https://doi.org/10.1126/science.803714
Abstract
Proteins were selectively solubilized from human erythrocyte membranes with deoxycholate. After ultracentrifugation and preliminary fractionation procedures, the detergent was removed from the soluble membranes by Bio-Beads SM-2 and dialysis against 5 millimolar magnesium chloride. Reaggregation took place with the apparent formation of vesicles which showed serologically specific Rh antigen activity.Keywords
This publication has 19 references indexed in Scilit:
- A simple procedure for removal of triton X-100 from protein samplesAnalytical Biochemistry, 1973
- Reconstitution of biological membranesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1972
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Another Example of Phenotype RhnullTransfusion, 1970
- Changes in the properties of human erythrocyte membrane protein after solubilization by butanol extractionBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathioneBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1967
- Heterogeneity of Water-Soluble Structural Components of Human Red Cell MembraneNature, 1965
- Purification and properties of a lysolecithinase from pancreasBiochemical Journal, 1953
- An Agglutinable Factor in Human Blood Recognized by Immune Sera for Rhesus BloodExperimental Biology and Medicine, 1940
- AN UNUSUAL CASE OF INTRA-GROUP AGGLUTINATIONJAMA, 1939