Abstract
Covalently, cross-linked immune complexes were prepared with multivalent 2-nitro-4-azidophenyl X human serum albumin (NAP X HSA) and antibodies to NAP at five times antigen excess. After purification with gel filtration, affinity chromatography with antigen-agarose column, and addition of the hapten, 9.5% of the antibodies dissociated from the complexes by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. After injection of these cross-linked immune complexes into mice, glomeruli stained for the complexes by immunofluorescence microscopy for only a few hours and electron-dense deposits were not detected. In contrast, when the same immune complexes with comparable lattice but without covalent cross-linking were administered to a second group of mice, the initial deposition by immunofluorescence was comparable and then increased to extensive deposits that persisted to 96 h. In this second group of mice extensive electron-dense deposits evolved. These observations supported the conclusion that the immune complexes initially deposited from circulation must undergo rearrangement to persist and to form electron-dense deposits in glomeruli. The covalently cross-linked immune complexes existed in glomeruli only for a short period of time since these complexes could not rearrange.
MeSH Terms
Animals
Antigen-Antibody Complex/analysis,immunology
Binding Sites, Antibody
Cross-Linking Reagents/pharmacology
Electrophoresis, Polyacrylamide Gel
Female
Fluorescent Antibody Technique
Humans
Kidney Glomerulus/immunology,ultrastructure
Mice
Mice, Inbred C57BL
Nitrophenols/immunology
Phenylacetates
Rabbits
Serum Albumin/immunology
Chemicals
Antigen-Antibody Complex
Cross-Linking Reagents
Nitrophenols
Phenylacetates
Serum Albumin
4-hydroxy-5-nitrophenyl acetic acid
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mannik M
Agodoa L Y
David K A
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11 references, click to expand
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