在含有2,4-二硝基苯基残基的吸附剂上对酸性蛋白酶和胰凝乳蛋白酶进行色谱分析。
Chromatography of acid proteinases and chymotrypsin on a sorbent containing 2,4-dinitrophenyl residues.
作者信息
Stepanov V M, Lavrenova G I, Borovikova V P, Balandina G N
出版信息
J Chromatogr. 1975 Feb 12;104(2):373-7. doi: 10.1016/s0021-9673(00)91861-2.
A sorbent obtained by treatment of cyanogen bromide-activated Sepharose 4B with mono-N-DNP-hexamethylenediamine has been shown to be effective in the affinity chromatography of pepsin, pepsinogen and acid proteinase from Aspergillus awamori. It is considered that 2,4-dinitrophenyl residues of the sorbent interact specifically with the hydrophobic zone of the enzyme, which may belong to the substrate binding site. The chromatography of chymotrypsin on the same sorbent supports this assumption.
用单 - N - DNP - 六亚甲基二胺处理溴化氰活化的琼脂糖凝胶4B所得到的吸附剂，已证明在对来自泡盛曲霉的胃蛋白酶、胃蛋白酶原和酸性蛋白酶进行亲和层析时是有效的。据认为，该吸附剂的2,4 - 二硝基苯基残基与酶的疏水区域特异性相互作用，该疏水区域可能属于底物结合位点。在同一吸附剂上进行的胰凝乳蛋白酶层析支持了这一假设。
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