Insulin and anti-insulin antibody interaction. Evidence for the formation of 7 S and 10 S structures.

Abstract:

:The clearing of monoclonal and polyclonal and anti-insulin antibodies from homogeneous solutions at 100,000 X g was used to estimate the size of soluble insulin-antibody complexes at physiologic concentrations. Monoclonal antibodies cleared as a uniform population of 6.6 S independent of the insulin concentration. Polyclonal antibodies cleared as 6.6 S monomers at saturation and as 10 S particles when the amount of insulin bound decreased, suggesting that a soluble complex with two antibodies was formed. An increase of the affinity and a decrease of antibody valency can be related to the complex formation. The binding affinity of polyclonal sera depends on the composition of the affinities of the IgG monomers and on their ability to form 10 S complexes. The formation of insulin-antibody dimers precludes cross-linking and precipitation. Both types of insulin-antibody complexes have been found in the sera from patients treated with bovine insulin.

journal_name

Diabetes

journal_title

Diabetes

authors

Petersen KG,Storch MJ,Rother K,Licht T,Kerp L

doi

10.2337/diab.34.8.799

subject

Has Abstract

pub_date

1985-08-01 00:00:00

pages

799-802

issue

8

eissn

0012-1797

issn

1939-327X

journal_volume

34

pub_type

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