Abstract
The first nucleolar protein to be isolated in an electrophoretically homogeneous state was extracted with 0.4 N H 2SO 4 from isolated nucleoli of Novikoff hepatoma ascites cells and separated as a slow moving distinct band by slab gel electrophoresis from the remaining nucleolar proteins. This protein, which has a molecular weight of approximately 65,000, accounts for 3–5% of the total acid-extractable nucleolar proteins. Its ratio of acidic to basic amino acids is 1.7 and serine is its amino terminal amino acid, as shown by thin layer chromatography of its dinitrophenyl derivative. The same band was also found in electrophoretic patterns of acid-extractable proteins in nucleoli of normal and thioacetamide-treated rat liver.
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