[Determination of binding constants of antibodies fractionated according to their affinity to insulin].
The number of populations of antibodies differing in their affinity for insulin was determined in guinea pig antiserum. The antibody fractions differing in their affinity were obtained by affinity chromatography on an antigenic sorbent. Elution with a stepwise pH gradient from 4 to 2 differing in the number and form of the steps resulted in 10 fractions of antibodies obtained from individual animal sera. The binding constants of fractionated antibodies were determined by a bioluminescent immunocofactor method. With a change in elution pH from 4 to 2, the equilibrious binding constant of antibodies increased from 10(6) to 5 X 10(9) M-1.
D000818:Animals; D000936:Antigen-Antibody Complex / Q000032:analysis*; D005591:Chemical Fractionation; D002846:Chromatography, Affinity; D006168:Guinea Pigs; D007074:Immunoglobulin G / Q000032:analysis; D007163:Immunosorbent Techniques; D007330:Insulin Antibodies / Q000032:analysis / Q000276:immunology*; D007700:Kinetics
D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D007330:Insulin Antibodies
Opredelenie konstant sviazyvaniia antitel, fraktsionirovannykh po srodstvu k insulinu.