Phosphorylation of Chromatin-associated Proteins in Lemna and Hordeum1

AUTOR(ES)

van Loon, L. C.

RESUMO

Sterile embryos of barley (Hordeum vulgare) and cultures of Lemna perpusilla have been labeled with 32Pi and the chromatin proteins prepared and separated by acid-urea and sodium dodecyl sulfate gel electrophoresis. Under these conditions chromatin proteins became labeled and the gel radioactivity profiles which were complex indicated a probable minimum of 15 to 20 proteins phosphorylated with molecular weights ranging from 104 to 105. The majority of the radioactivity, 80 to 90% of the total, is found in the acidic protein fraction and this can be recovered as serine phosphate after partial acid hydrolysis.

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