By Hsueh Jei Li
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Additional resources for Chromatin and Chromosome Structure
And Weiskopf, M. (1973) Biochemistry 1 2 , 1763. Reprinted with permission of the American Chemical Society. agree with 50-60% bound by these latter histones as determined by thermal denaturation (31). In fact, the above suggestion is supported by the recent reports (60a,60b) that histone Hi does not belong to the basic subunit in nucleaseresistant particles as to be discussed in Section V I I I . Based upon the above evidence and discussion, the figure of 8 0 % for DNA bound by histones in chromatin as determined by thermal denaturation (at least in pea bud and calf thymus) (30,31) is a more reliable value than that of the 50% determined by polylysine binding and nuclease digestion (39).
And Crane-Robinson, C. (1975) Biochemistry 14, 3391. Reprinted wi ssion of the American Chemical Society. HSUEH JEI LI different from the model shown in Fig. 13 which suggests the presence of 3-sheet in multiple chains of histone H 4 . Histone H 4 is the only histone molecule having been studied so extensively. Although some understanding of conformational changes and interactions in this histone have been developed, a detailed description of its structure is still difficult. The studies of fragments of histone H4 (47,49) are interesting and useful.
The above concept of the conditions for biphasic melting was found to be incompatible with the thermal denaturation results found both in pea bud chromatin and in partially dehistonized chromatin. 5 χ 10"" M EDTA, pH 8 . 0 ) , both native chromatin and partially dehistonized chromatin from pea bud show two chracteristic melting bands at 66 and 81°C. The amplitude of these two melting bands was proportionately decreased when histones were removed by H2SO4, NaCl or MgCl2The two characteristic phases of melting in histone-bound DNA in chromatin could not be satisfactorily interpreted using the concept of cooperative binding of histones to DNA in native and in salt or acid-treated chromatin.