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• W2023673716 abstract "Bispecific antisera were prepared to a mixture of thylakoid membrane polypeptides 4.1 and 4.2. The identity of these polypeptides as the α and β subunits of coupling factor1 (CF1) was established based on the cross-reactivity of the antisera toward CF1 from peas and by an analysis of the thm-24 mutant of Chlamydomonas which lacks the CF1 ATPase. Photochemical labeling of thylakoid membranes with hydrophobic and hydrophilic fluorescent probes indicated that these polypeptides did not significantly penetrate the membrane bilayer. Immunoprecipitation of the translation products of thylakoid-bound and soluble ribosomes showed the thylakoids to be the major site of synthesis of the polypeptides. Immunoprecipitation of the products of translation of total cellular RNA in a reticulocyte lysate showed no evidence for substantially higher molecular weight precursors. Further analysis of the thylakoid-bound synthesis of α and β revealed that some of the in vitro synthesized polypeptides had been incorporated into the CF0CF1 complex based on their release from membranes with trypsin and copurification with the CF0-CF1 ATPase." @default.
• W2023673716 created "2016-06-24" @default.
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• W2023673716 creator A5079244154 @default.
• W2023673716 date "1985-02-01" @default.
• W2023673716 modified "2023-09-25" @default.
• W2023673716 title "In vitro synthesis and assembly of the peripheral subunits of coupling factor CF1 (α and β) by thylakoid-bound ribosomes" @default.
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• W2023673716 doi "https://doi.org/10.1016/0003-9861(85)90273-5" @default.
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