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- W1969011644 abstract "Abstract The P-700-chlorophyll a-protein complex (F60) isolated previously by a nondetergent method (Huang, C. and Berns, D.S. (1983) Arch. Biochem. Biophys. 220, 145–154) has been treated with the anionic detergent sodium dodecyl sulfate (SDS), and the two resulting fractions, designated (for heavy) H and (for light) L, were separated by chromatography on a Sephacryl S-200 column. After removing detergent, the isolated H-fraction contains about 43 chlorophylls per P-700 molecule. At −196°C, the fluorescence emission peak of the H-fraction is at 715 nm; in the presence of detergent a major 677 nm and a minor 720 nm maximum are observed. The low-temperature emission maximum of the L-fraction is shifted from 686 to 677 nm in the presence of detergent. Two bands at approx. 696 and 654 nm are observed in the chemically induced difference spectra of F60 and the H-fraction in SDS-Tris buffer, but principally one band at 654 nm is observed in the L-fraction. After exhaustive dialysis in Tris buffer, the major 696 nm band is dominant in all samples and there is a great attenuation of the 654 nm band. The polypeptide composition of F60 and the H-fraction are similar while the L-band consists of polypeptides lower than 20 kDa. The amino acid composition of F60 and its two components (H and L) is also reported. Sedimentation-velocity studies indicate that in SDS-Tris buffer the H-fraction contains two species, 2.5 and 10.1 S, and in Tris buffer one species, 14.7 S, while the L-fraction contains one species, 2.5 S, with or without the detergent. The results presented here suggest that the heart of Photosystem I is mainly localized in the H-fraction and that the light-harvesting chlorophyll-protein complex is in the L-fraction." @default.
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- W1969011644 date "1984-04-01" @default.
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- W1969011644 title "Characterization of components of P-700-chlorophyll a-protein complex from a blue-green alga, Phormidium luridum" @default.
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- W1969011644 doi "https://doi.org/10.1016/0005-2728(84)90152-x" @default.
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