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A Monoclonal Antibody Affects Chromophore Apoprotein Interactions of Phytochrome A
Author(s) -
Nakazawa Miki,
Moriuchi Naoko,
Wada Naoko,
Hirose Tetsuya,
Tokutomi Satoru,
Manabe Katsushi
Publication year - 1997
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1997.tb01919.x
Subject(s) - chromophore , phytochrome , monoclonal antibody , chemistry , biophysics , antibody , photochemistry , biology , botany , red light , immunology
— A monoclonal antibody designated Mep‐1 was raised against phytochrome A from pea ( Pisum sativum L.). The binding of this antibody (class IgG 1 ) to partially degraded phytochrome (114 kDa) caused a considerable increase in the far‐red peak at the red‐light‐induced stationary state. The effect reached a plateau value when the antibody and phytochrome were present in approximately equimolar amounts. The dark transformation of the far‐red‐light‐absorbing form to the red‐light‐absorbing form of the 114 kDa phytochrome was inhibited by the addition of the antibody. However, binding of the antibody to the undegraded 121 kDa phytochrome had no effects on the spectrum of the red‐light‐induced steady state. The site at which the antibody bound to phytochrome was determined to be between amino acid residues 256 and 383 of pea phytochrome A. This is the first report of a monoclonal antibody that enhances the far‐red absorption of phytochrome in the red‐light‐induced photostationary state.