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金属离子促进蛋白质与固定化三嗪染料亲和吸附剂的结合。

Metal ion-promoted binding of proteins to immobilized triazine dye affinity adsorbents.

作者信息

Hughes P, Lowe C R, Sherwood R F

出版信息

Biochim Biophys Acta. 1982 Jan 4;700(1):90-100. doi: 10.1016/0167-4838(82)90296-5.

DOI:10.1016/0167-4838(82)90296-5
PMID:6895701
Abstract

Low concentrations of metal ions, particularly those of the first row transition series such as Zn2+, Co2+, Mn2+, Ni2+, Cu2+, and, to a lesser extent, the group IIA ions, Ca2+ and Mg2+, promotes binding of carboxypeptidase G2, alkaline phosphatase and yeast hexokinase to immobilized Procion Red H-8BN, Procion Yellow H-A and Cibacron Blue F3G-A respectively. The binding of ovalbumin to immobilized Cibacron Blue F3G-A and Procion Orange MX-G is selectively enhanced in the presence of AI3+. With ovalbumin and alkaline phosphatase, the effect is almost totally specific for both the metal ion and dye, whereas with carboxypeptidase G2 and hexokinase, metal ions such as Co2+, Ni2+, Mn2+, Cu2+, Ca2+ and Mg2+ also promote binding to varying degrees. Almost all other monovalent and trivalent metal ions appear to be ineffective. Metal ion-bound enzymes can subsequently be eluted with appropriate chelating agents of the amine, aminocarboxylate or substituted pyridine classes.

摘要

低浓度的金属离子,特别是第一排过渡系列的那些离子,如Zn2+、Co2+、Mn2+、Ni2+、Cu2+,以及在较小程度上的IIA族离子Ca2+和Mg2+,分别促进羧肽酶G2、碱性磷酸酶和酵母己糖激酶与固定化的普施安红H - 8BN、普施安黄H - A和汽巴克隆蓝F3G - A的结合。在Al3+存在的情况下,卵清蛋白与固定化的汽巴克隆蓝F3G - A和普施安橙MX - G的结合被选择性增强。对于卵清蛋白和碱性磷酸酶,这种效应几乎对金属离子和染料都具有完全特异性,而对于羧肽酶G2和己糖激酶,Co2+、Ni2+、Mn2+、Cu2+、Ca2+和Mg2+等金属离子也会不同程度地促进结合。几乎所有其他单价和三价金属离子似乎都没有效果。金属离子结合的酶随后可用胺类、氨基羧酸盐类或取代吡啶类的适当螯合剂洗脱。

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