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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Dec;81(23):7343–7347. doi: 10.1073/pnas.81.23.7343

Monoclonal antibodies to human type IV collagen: useful reagents to demonstrate the heterotrimeric nature of the molecule.

B F Odermatt, A B Lang, J R Rüttner, K H Winterhalter, B Trüeb
PMCID: PMC392142  PMID: 6209713

Abstract

Monoclonal antibodies (mAbs) have been prepared against type IV collagen isolated from human kidney. Two mAbs, designated CIV 22 and CIV 16, were extensively characterized. CIV 22 reacted only with native type IV collagen, whereas CIV 16 also bound to fragments derived from the alpha 1(IV) chain after reduction and alkylation of the molecule. Therefore, CIV 22 recognizes a conformational epitope on the triple helical type IV collagen, whereas CIV 16 binds to a sequential determinant in the carboxyl-terminal half of the alpha 1(IV) chain. By immunofluorescence, typical basement membrane structures were stained with both mAbs on frozen sections of different human organs. The mAbs were used to investigate the chain composition of type IV collagen. Radiolabeled type IV collagen bound to CIV 22, proving its triple helical configuration. These native probes, containing both the alpha 1(IV) and the alpha 2(IV) chains, also bound to CIV 16. Since CIV 16 does not react with the isolated alpha 2(IV) chain, both chains must be arranged in a single triple helical molecule (heterotrimer).

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These references are in PubMed. This may not be the complete list of references from this article.

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