[Studies of DNP protein dissociation in the presence of norepinephrine]

Calf thymus DNP dissociation was studied by sepharose 2B gel-chromatography as well as by oxyapatite ion-exchange chromatography. The degree of dissociation was estimated by protein content in the chromatography peaks. Intact DNP and DNP incubated with norepinephrine were filtered simultaneously through two identical columns. In the presence of norepinephrine a partial deproteinization was observed. This effect has some specificity, namely, it was considerably lower in the presence of tyrosine, and was absent when the norepinephrine structure was changed. On the basis of the available data on the norepinephrine ability to form chelatic complexes with polyvalent metals and comparing the deproteinizing effect of norepinephrine and EDTA it was assumed that the norepinephrine dissociating effect was due to its binding with cations incorporated into the DNP complex structure.