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- W2013156518 abstract "Chloroplasts isolated from leaves of Vicia faba L. were capable of incorporating [35S]methionine in the light into a number of thylakoid-bound polypeptides. Among these products, two polypeptides co-migrated in lithium dodecylsulfate polyacrylamide gel electrophoresis with the constituting polypeptides of the light-harvesting chlorophyll a/b-protein complex II. After labelling of chloroplasts in vitro, chlorophyll-protein complex II was precipitated with a monospecific antiserum as revealed by gel electrophoresis. The immunoprecipitate was shown to be radioactive by fluorography. One-dimensional peptide mapping of the products of hydrolysis with S. aureus protease confirmed that the radioactivity was an integral part of the apoprotein of the chlorophyll-protein complex II. Incorporation of [35S]methionine into this complex by isolated chloroplasts was inhibited by D-threo-chloramphenicol but not by cycloheximide. Labelling did not occur if the chloroplasts were isolated from leaves which had been pretreated with α-amanitin. It is concluded that in intact isolated Vicia faba chloroplasts chlorophyll-protein complex II is synthesized from mRNA of nuclear origin." @default.
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- W2013156518 date "1983-11-01" @default.
- W2013156518 modified "2023-09-24" @default.
- W2013156518 title "Biosynthesis and Membrane Insertion of a Chlorophyll a/b-binding Protein by Isolated Vicia faba L., Chloroplasts" @default.
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- W2013156518 doi "https://doi.org/10.1016/s0044-328x(83)80143-3" @default.
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