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Protein synthesis etioplasts

Analysis of the products of etioplast protein synthesis by SDS polyacrylamide gel electrophoresis reveals a pattern of labeled peaks (Fig. 12) very similar to the pattern produced by isolated chloroplasts (Fig. 3) peaks A to F can be recognized, and all are removed by digestion with pronase. The most highly labeled peak, B, runs coincident with the large subunit of Fraction I protein and is released in soluble form when etioplasts are lysed in hypotonic buffer and centrifuged at 105,000g for 1 h. The other labeled peaks sediment with the membrane fraction. We conclude from these results that etioplasts probably make the same range of proteins as do chloroplasts. [Pg.268]

One difference that we found between protein synthesis by etioplasts and that by chloroplasts is in the relative labeling of peaks B and D. In chloroplasts, these peaks contain similar amounts of radioactivity in most experiments, with peak B sometimes being slightly more labeled than peak D. However, in etioplasts peak B is by much the most highly labeled component. When etiolated pea plants are greened under continuous light over 4 days, the products of protein synthesis by plastids—isolated at inter-... [Pg.268]


See other pages where Protein synthesis etioplasts is mentioned: [Pg.372]    [Pg.2521]    [Pg.2523]    [Pg.2590]    [Pg.262]    [Pg.267]    [Pg.268]    [Pg.226]    [Pg.163]    [Pg.267]   
See also in sourсe #XX -- [ Pg.267 , Pg.268 ]




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Etioplasts

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