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Monoclonal antibody ARC MAC 50.1 binds to a site on the phytochrome molecule which undergoes a photoreversible conformational change
Author(s) -
Thomas Brian,
Penn Susan E.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80155-7
Subject(s) - phytochrome , monoclonal antibody , chemistry , biophysics , arc (geometry) , conformational change , peptide , binding site , avena , antibody , biochemistry , biology , botany , red light , geometry , mathematics , immunology
Monoclonal antibody from rat hybridoma cell line ARC MAC 50.1 binds more strongly to Pfr than to Pr in a sandwich ELISA of phytochrome in crude Avena sativa L. extracts or highly purified Avena phytochrome. Discrimination is not a consequence of differential modification of Pr and Pfr during the assay. Loss of a 6 kDa peptide from the N‐terminal end of the phytochrome apoprotein during purification does not prevent discrimination. Neither is preferential binding to Pfr a consequence of a steric interaction between ARC MAC 50.1 and the antibody used with it in the sandwich ELISA. It is concluded that the binding site for ARC MAC 50.1 undergoes a reversible conformational change upon photoconversion and may thus represent a functional region of the phytochrome molecule.