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IDENTIFICATION OF TRYPTIC CHROMOPEPTIDES OF PHYTOCHROME ON SODIUM DODECYL SULFATE GELS: IMPLICATIONS FOR STRUCTURE
Author(s) -
Stoker Blanche M.,
McEntire Kerry,
Roux Stanley J.
Publication year - 1978
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.1751-1097.1978.tb07651.x
Subject(s) - sodium dodecyl sulfate , phytochrome , trichloroacetic acid , chemistry , chromatography , absorption (acoustics) , sodium , polyacrylamide , protein subunit , biophysics , biochemistry , biology , botany , optics , red light , organic chemistry , polymer chemistry , physics , gene
— After electrophoresis on sodium dodecyl sulfate polyacrylamide gels, bleached chromopeptides of phytochrome can have their blue color restored by soaking the gels in 20% trichloroacetic acid. The blue bands have a broad absorption maximum between 630 and 655 nm, characteristic of denatured phytochrome. The restored color retains most of its intensity for up to 2 h, but gradually bleaches again until it disappears completely within 24 h. This visualization method is used to identify the number and sizes of phytochrome chromopeptides produced by limited tryptic digestion. The results reveal some structural requirements for photoreversibility and are consistent with a model of phytochrome structure that predicts a high degree of symmetry within the native subunit.