| Abstract: | Rat liver chromatin was moderately digested by micrococcal nuclease and analysed by centrifugation in isokinetic sucrose gradients and electron microscopy. Two classes of particles sedimenting with about 33S and 60S were characterized. Kinetics of their appearance and disappearance during progressive digestion suggests that they represent monomers and dimers cleaved from a higher order (supranucleosomal) structure of chromatin. Biochemical and electron microscopical results suggest that the monomers and dimers contain eight and sixteen nucleosomes, respectively, which are densely packed into 23 nm (monomer) and 29 nm (dimer) globules. |
