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
Diabetesjournal_title
Diabetesauthors
Petersen KG,Storch MJ,Rother K,Licht T,Kerp Ldoi
10.2337/diab.34.8.799subject
Has Abstractpub_date
1985-08-01 00:00:00pages
799-802issue
8eissn
0012-1797issn
1939-327Xjournal_volume
34pub_type
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