Studies on chromatin. II. Isolation and characterization of chromatin subunits.
Earlier findings /1-10/ bearing on a subunit organization of chromatin were confirmed and in some points detailed. Besides this, a large-scale isolation of chromatin subunits; their protein composition, electron microscopic appearance and CsCl banding pattern are described. Although the purified chromatin subunit contains all five histones, the relative content of histone H1 i in it is two times lower than that in the original chromatin. tit is shown that a mild digestion of chromatin with staphylococcal nuclease produced not only separate chromatin subunits and their "oligomers' but also deoxyribonucleoprotein particles which sediment more slowly than subunits. It appears that these particles and subunits are produced from different initial structures in the chromatin. Finally, a crystallization of the purified chromatin subunit as a cetyltrimethyl ammonium salt is described.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000032:analysis; D002499:Centrifugation, Density Gradient; D002843:Chromatin / Q000302:isolation & purification / Q000648:ultrastructure; D002850:Chromatography, Gel; D003460:Crystallization; D004273:DNA, Neoplasm / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000032:analysis; D007700:Kinetics; D051379:Mice; D008836:Micrococcal Nuclease; D008854:Microscopy, Electron; D009698:Nucleoproteins / Q000032:analysis; D013997:Time Factors
D002843:Chromatin; D004273:DNA, Neoplasm; D006657:Histones; D009698:Nucleoproteins; D008836:Micrococcal Nuclease