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- W2072912209 abstract "Thylakoids isolated from pine chloroplasts were solubilized by sodium dodecyl sulphate and the polypeptides were separated by polyacrylamide gel electrophoresis. The chlorophyll-protein complexes, P700-CPa1 and LH-CPa/b, had apparent molecular weights of 92,000 and 25,000, respectively. When the chlorophyll of P700-CPa1 was extracted or photobleached, the apoprotein of P700-CPa1 appeared as a pronounced peak in the polypeptide scan profile. The molecular weight of the apoprotein was 70,000. During autumn and winter the complex P700-CPa1 was destroyed. This was primarily caused by bleaching of chlorophyll, as the 70,000 apoprotein increased in the scan profile when the complex P700-CPa1 decreased. The winter destruction of P700-CPa1 was less pronounced in old needles than in young. Freezing of frost-hardened seedlings did not change the polypeptide scan profile, unless the temperature was lowered below the frost-killing point followed by thawing and post-treatment in light or darkness above 0°C. Again the main destruction occurred in the P700-CPa1 complex, but in this case no significant increase of the apoprotein was observed. These alterations in the polypeptide scan profile of frost-killed needles were not caused by the low temperature treatment as such, but they occurred after thawing of the needles." @default.
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- W2072912209 date "1978-11-01" @default.
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- W2072912209 title "Effects of Season and Low Temperature on Polypeptides from Thylakoids Isolated from Chloroplasts of Pinus silvestris" @default.
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- W2072912209 doi "https://doi.org/10.1111/j.1399-3054.1978.tb08636.x" @default.
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