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Studies on Adrenal Histones

CHARACTERIZATION, BIOSYNTHESIS, ENZYMATIC PHOSPHORYLATION, AND ACETYLATION OF HISTONES FROM A HUMAN ADRENAL CARCINOMA

From the ¹ From the Department of Biochemistry and Medicine, Northwestern University Medical School and Chicago Wesley Memorial Hospital, Chicago, Illinois 60611

Histones F1, F2a, F2b, and F3 were isolated from a human adrenal carcinoma. The fractions were purified by chromatography on carboxymethyl Sephadex and characterized by amino acid analysis and disc electrophoresis. The histones were comparable to calf thymus histones in amino acid composition and electrophoretic patterns. Adrenal carcinoma F3 showed a more complex electrophoretic pattern than calf thymus F3. To study biosynthesis, phosphorylation, and acetylation of histones, adrenal slices were incubated with lysine-³H, Na₃³²PO₄, and sodium acetate-¹⁴C at intervals between 5 and 120 min. The rate of histone biosynthesis as measured by lysine-³H incorporation was similar for the F1 and F2b fractions and did not increase further after 30-min incubation time. The arginine-rich histone F3 showed the highest rate of lysine-³H uptake, and its biosynthetic rate was about 16 times higher than the rate of F1 biosynthesis. The incorporation of Na₃³²PO₄ and sodium acetate-¹⁴C increased with time in all histone fractions. The rate of phosphorylation and acetylation as indicated by the specific activities of the histones was similar in the F1, F2a, and F2b fractions. The F3 histone showed the highest rate of ³²P and ¹⁴C uptake. However, comparison of the acetylation and phosphorylation of the histones in relation to their biosynthetic rate suggests that the turnover of histone-bound phosphate-³²P and acetate-¹⁴C is faster in the lysine-rich fractions F1 and F2b than in the arginine-rich histones.

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