NUCLEAR PROTEINS .3. FIBRILLAR NATURE OF NUCLEAR MATRIX
NUCLEAR PROTEINS .3. FIBRILLAR NATURE OF NUCLEAR MATRIX
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DOI:
10.1016/0014-4827(76)90271-8
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发表时间:
1976-01-01
影响因子:
3.7
通讯作者:
OKADA, TA
中科院分区:
文献类型:
--
作者:
COMINGS, DE;OKADA, TA
The nuclear matrix of mouse liver nuclei was examined after extraction of the chromatin with high salt, DNase and Triton X-100. The residual nuclear matrix is composed of a nuclear pore-lamina complex, fibrillar nucleoli and intranuclear matrix. Whole mount EM shows that a portion of the nuclear matrix is composed of 20-30 .ANG. protein fibers called matrixin. The fibers may associate to form larger 100-300 .ANG. fibers. When mouse testicular cells were used, intact synaptonemal complexes and the sex vesicle were intimately associated with the matrix and may be composed of matrixin. SDS gel electrophoresis of the matrix shows 3 major polypeptides of 65,000, 67,000 and 68,000 D. Several observations suggest DNA is attached to the matrix at many sites throughout the nucleus. The matrix may play a role in the arrangement of chromatin into the chromomeres of meiotic and mitotic chromosomes.