酸性脱氧核糖核酸酶的一种蛋白质抑制剂。
A protein inhibitor of acid deoxyribonucleases.
作者信息
Lesca P, Paoletti C
出版信息
Proc Natl Acad Sci U S A. 1969 Nov;64(3):913-9. doi: 10.1073/pnas.64.3.913.
A protein extracted and partially purified (about 100-fold) from mouse liver is able to inhibit the acid DNases from different tissues and species, whereas pancreatic DNase and E. coli endonuclease I are not inhibited. The acid DNase displays typical Michaelis-Menten kinetics in the absence of this inhibitor, but the kinetics become sigmoidal in its presence. The existence of a DNase-inhibitor complex is demonstrated by physicochemical experiments. Moreover, the inhibitor is able to reactivate the DNase treated by urea, probably through a reassociation of the inactive monomers to a dimeric state. An allosteric model in which the DNase-inhibitor complex is composed of catalytic (DNase) and regulatory (inhibitor) subunits could explain these data.
从小鼠肝脏中提取并部分纯化（约100倍）的一种蛋白质能够抑制来自不同组织和物种的酸性脱氧核糖核酸酶，而胰腺脱氧核糖核酸酶和大肠杆菌内切核酸酶I则不受抑制。在没有这种抑制剂的情况下，酸性脱氧核糖核酸酶表现出典型的米氏动力学，但在其存在时动力学变为S形。通过物理化学实验证明了脱氧核糖核酸酶-抑制剂复合物的存在。此外，该抑制剂能够使经尿素处理的脱氧核糖核酸酶重新激活，可能是通过无活性单体重新缔合形成二聚体状态。一种变构模型，其中脱氧核糖核酸酶-抑制剂复合物由催化（脱氧核糖核酸酶）和调节（抑制剂）亚基组成，可以解释这些数据。
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