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- W2014891612 abstract "Abstract The photosynthetic complex, Photosystem I, of the thermophilic cyanobacterium Phormidium laminosum was found to be highly resistant to denaturation by ionic and non-ionic detergents including SDS. This property was exploited to allow the preparation by sucrose density gradient centrifugation and by SDS-poly-acrylamide gel electrophoresis of several protein complexes containing the PS I reaction centre components, chlorophyll a and carotenoid. In this report I have focused attention on the three most abundant complexes of estimated molecular masses of 450, 150 and 105 kDa. An initial description of the complexes is presented. The 105 kDa complex resembles plant CP-1 with a very low quantum efficiency for stable charge separation when compared with the 150 and 450 kDa complexes. This deficiency was associated with the loss of two low-molecular-weight polypeptides from the 105 kDa complex. The 450 kDa complex can be separated from the other complexes by centrifugation in a sucrose density gradient, and was found to be the most stable of the complexes in the presence of SDS. All three complexes contain roughly equivalent amounts of the reaction centre component P-700, suggesting that the 450 kDa complex is a multimer of the 150 kDa complex." @default.
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- W2014891612 date "1987-09-01" @default.
- W2014891612 modified "2023-09-27" @default.
- W2014891612 title "Investigation of highly stable Photosystem I chlorophyll-protein complexes from the thermophilic cyanobacterium Phormidium laminosum" @default.
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- W2014891612 doi "https://doi.org/10.1016/0005-2728(87)90031-4" @default.
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