Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Interaction /sup 125/I-protein A with erythrocyte-bound IgG

Journal Article · · J. Lab. Clin. Med.; (United States)
OSTI ID:5403224
The molar combining ratio of /sup 125/I-PrA to RBC-bound /sup 125/I-labeled IgG anti-D was 0.72 +/- 0.044. There was a significant decrease in the PrA-to-IgG combining ratio when anti-D was bound to protease-modified RBCs or to unmodified RBCs sensitized at low ionic strength, 0.49 +/- 0.034 and 0.56 +/- 0.006, respectively. These findings indicate that the interaction of RBC-bound IgG with PrA may be influenced by alterations in membrane structure, surface density, and distribution of the IgG receptor and possibly other steric factors. The quantity of RBC-bound IgG on RBCs sensitized with unlabeled serum anti-D and anti-Kell could be quantitatively assessed and correlated with antiglobulin agglutinability. Unlabeled alloantibodies were detected with the /sup 125/I-PrA at IgG densities lower than those detectable with the standard antiglobulin test. /sup 125/I-PrA, in contrast to the antiglobulin reaction, has the potential of providing increased sensitivity as well as quantitative data in assessing IgG alloantibody- or autoantibody-sensitized RBCs.
Research Organization:
Department of Pathology, School of Medicine, University of California, San Diego, La Jolla
OSTI ID:
5403224
Journal Information:
J. Lab. Clin. Med.; (United States), Journal Name: J. Lab. Clin. Med.; (United States) Vol. 99:3; ISSN JLCMA
Country of Publication:
United States
Language:
English