Fractionation of isolated brain nuclei previously reacted with (125)I-labelled S-100 showed that most of the specifically bound radioactivity associated with the nuclear membranes and the nucleoli. Labelling of nucleoli, which indicates the entrance of (125)I-labelled S-100 into the nucleus, was observed at 37 percent C, but not at 0-4 percent C. When tested separately for (125)I-labelled S-100 specific binding, both the nuclear membranes and the nucleoli were found to bind (125)I-labelled S-100 in a biphasic manner, the binding displaying a high affinity and a low affinity component, as observed with intact nuclei. However, the binding to nuclear membranes was largely irreversible, while that to nucleoli was fully reversible after any association time.
Subnuclear distribution of the S-100 protein specific binding sites in rat brain
DONATO, Rosario Francesco
1981
Abstract
Fractionation of isolated brain nuclei previously reacted with (125)I-labelled S-100 showed that most of the specifically bound radioactivity associated with the nuclear membranes and the nucleoli. Labelling of nucleoli, which indicates the entrance of (125)I-labelled S-100 into the nucleus, was observed at 37 percent C, but not at 0-4 percent C. When tested separately for (125)I-labelled S-100 specific binding, both the nuclear membranes and the nucleoli were found to bind (125)I-labelled S-100 in a biphasic manner, the binding displaying a high affinity and a low affinity component, as observed with intact nuclei. However, the binding to nuclear membranes was largely irreversible, while that to nucleoli was fully reversible after any association time.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.