Abstract
Histones and protamines are present in animal cell nuclei as basic nuclear proteins associated with deoxyribonucleic acid. They are known to be inhomogeneous and probably consist of definite amounts of several components which are very similar in their nature and structure. The significance of the heterogeneity of these basic nuclear proteins has not yet been completely elucidated, though some particular activity in controlling DNA-dependent biosynthesis is sometimes attributed to each component of the histones.
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Alumina for chromatography (Wako Pure Chemicals Co. Ltd.), sieved between 200 to 300 mesh, was washed 5 times with tap water and 5 times with distilled water (adjusting pH of the supernatant to 4.3–4.7 with HCl), dried at 110 °C, and calcinated for 3–4 h over a Teclu burner. The alumina was then rinsed twice with 0.48 M K2HPO4, pH 9.0–9.2, and left overnight. The precipitate suspended in the buffer was transferred into a column.
This fraction proved later to have two components, I-I a and I-I b, in a molar ratio of 1 to 2, as shown by structural studies on peptides in thermolysin and Neutral Protease digests of I-I.
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© 1973 Springer-Verlag Berlin Heidelberg
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Ando, T., Yamasaki, M., Suzuki, K. (1973). Heterogeneity of Protamines and Homogeneous Molecular Species of Protamines. In: Protamines. Molecular Biology Biochemistry and Biophysics, vol 12. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46294-8_7
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DOI: https://doi.org/10.1007/978-3-642-46294-8_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-46296-2
Online ISBN: 978-3-642-46294-8
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