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Molecular Properties of Phytochrome [and Discussion]
M. Furuya, W. Haupt and M. Furuya
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
Vol. 303, No. 1116 (Oct. 18, 1983), pp. 361-375
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/2396555
Page Count: 15
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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 Pr and Pfr or between P659 and Pbl. Double flash-photolytic and low-temperature spectroscopic studies on the phototransformation pathways from Pr to Pfr and from Pfr to Pr 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 microcnvironmental 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.
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences © 1983 Royal Society