The Immunologic and Molecular Profiles of HLA Antigens Isolated from Urine
Open Access
- 1 January 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 118 (1) , 264-269
- https://doi.org/10.4049/jimmunol.118.1.264
Abstract
Human urine was shown to be a good source for the isolation of immunologically functional HLA-A9 antigens. The use of complex solubilization procedures can be avoided since the antigens are present in soluble form and are not complexes with membrane fragments. Purification in excess of 400-fold could be achieved by the application of cellulose ion exchange chromatography, isoelectric focusing, and acrylamide gel electrophoresis. The purified HLA-A9 antigen is composed of a glycoprotein of m.w. 38,000 and β2-microglobulin, a peptide of m.w. 12,000. HLA-A9 antigens isolated from urine proved to be immunologically functional since they not only reacted specifically with anti-HLA-A9 alloantibody but also elicited anti-HLA-A9 xenoantibodies. These antibodies when covalently attached to Sepharose 4B specifically bound HLA-A9 antigens isolated from both serum and urine.This publication has 0 references indexed in Scilit: