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SYNOPSIS. The basic proteins of Paramecium aurelia nucleus were extracted from isolated nuclei and deoxyribonucleoprotein (DNP) of such nuclei. About 35–40% of the nuclear protein, predominantly a lysine‐rich histone, is acid soluble. Five major components of the histone can be distinguished by polyacrylamide gel electrophoresis. Some components of Paramecium histone are similar to those of mammalian histones in their electrophoretic mobility, but they differ from the latter in the electrophoretic velocity and relative levels. The basic to acidic amino acid ratio of the histone from the ciliate is ∼1.1–1.5, and its amino acid composition resembles closely that of yeast histone. Through the use of Sephadex G‐200 gel filtration for purification of the histones extracted directly from isolated nuclei 2 basic proteins were resolved—component I, with an elution volume of 1.4, constitutes ∼20% and component II, with an elution volume of 1.9, ∼80%.

SYNOPSIS. Nuclei of Paramecium aurelia were isolated and purified by a new method involving the use of continuous or discontinuous sucrose gradient centrifugation. As judged from the DNA levels or nuclear counts in the purified samples, 21–22% of the nuclei were recovered by this method. The single density of the nuclei estimated on the basis of linear sucrose gradients was between 1.35 ± 0.01 and 1.36 ± 0.01. The average picogram quantities of total protein, DNA, and RNA per nucleus were 435, 62.2, and 51.2, respectively.