| Autor: |
Abraham, G.N., Clark, R.A., Vaughan, J.H. |
| Zdroj: |
Immunochemistry; March 1972, Vol. 9 Issue: 3 p301,IN1,30-304,IN1,31, 279p |
| Abstrakt: |
The binding properties and specificity of a purified homogeneous IgA rheumatoid factor have been determined. With the use of the equilibrium molecular sieving technique the interaction of the rheumatoid factor and a γG-Fc piece were studied. From the data a linear Scatchard plot was obtained and from this an antibody valence of 2 and an average intrinsic association constant [K(0)] 1·5 × 106L/M were calculated. The temperature dependence fo and the thermodynamic parameters governing the interaction were determined. Equivalent reactivity of the IgA rheumatoid factor with representative γG1, γG2and γG4myeloma proteins was demonstrated. Data is presented which supports the concept that the rheumatoid factor is reacting with a specific antigenic determinant present on the Fc region of these γG globulin molecules. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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