Mezzetti G, Monti M G, Moruzzi M S
Istituto di Chimica Biologica, Università di Modena, Italy.
Life Sci. 1988;42(22):2293-8. doi: 10.1016/0024-3205(88)90382-7.
The effect of polyamines on the catalytic domain of protein kinase C from rat brain was investigated. It was found that the addition of spermine strongly inhibited phosphorylation activity toward histone H1 as substrate. This tetramine, at millimolar concentrations, was most potently effective while triamines and diamines were almost uneffective, therefore the inhibitory action appeared to be structural specific. Data shown here suggest that polyamine by interacting with the catalytic domain of the enzyme may contribute to its regulation.
研究了多胺对大鼠脑蛋白激酶C催化结构域的作用。发现添加精胺可强烈抑制以组蛋白H1为底物的磷酸化活性。这种四胺在毫摩尔浓度下效果最为显著,而三胺和二胺几乎无效,因此这种抑制作用似乎具有结构特异性。此处所示数据表明,多胺通过与该酶的催化结构域相互作用可能有助于其调节。