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Article

Probing the activation stages of the RecA protein by monoclonal IgGs during the pairing of homologous DNA molecules.

The Journal of biological chemistry - 25 May 1990

Ikeda M, Makino O, Shibata T

Abstract excerpt

The biochemical properties of the RecA protein change in a stepwise manner with the binding of ATP and/or DNA during the course of the ATP-dependent formation of homologous joint molecules, which is assumed to be due to transition in the higher order structure. This transition was supposed to be detectable as changes in the affinity of the protein for monoclonal IgGs. In this study, we introduced an enzyme-linked...

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Share to Antibodies, Monoclonal
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Protein Binding

Share to Recombination, Genetic

Source

Identifiers

PMID: 2140364

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Probing the activation stages of the RecA protein by monoclonal IgGs during the pairing of homologous DNA molecules.PMID 2140364Read ↗

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