Molecular properties of phytochrome

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Abstract
Chromopeptides with molecular masses of ca . 114, 62, 56, 40, 39 and 33 kDa were prepared from pea phytochrome by limited proteolysis. Absorption and circular dichroism spectra were determined and proton uptake and release investigated. The data indicate how long the chromopeptide chain must be for photoreversible changes between P r and P fr or between P 659 and P bl . Double flash-photolytic and low-temperature spectroscopic studies on the photo-transformation pathways from P r to P fr and from P fr to P r of native and degraded chromopeptides were carried out under different conditions, demonstrating that the pool size of kinetically detectable intermediates in a sample changed reversibly depending upon monomer size, and microenvironmental factors such as pH and temperature. Six monoclonal antibodies against rye phytochrome and six against pea phytochrome were raised and investigated in terms of the sites of phytochrome determinants, species specificity, and influence on spectral and other molecular properties.