INTERACTION OF CATECHOL-2,3-DIOXYGENASE OF PSEUDOMONAS-PUTIDA WITH IMMOBILIZED HISTIDINE AND HISTAMINE

被引：15

作者：

HAUPT, K ^{[1
]}

VIJAYALAKSHMI, MA ^{[1
]}

机构：

[1] UNIV TECHNOL COMPIEGNE, TECHNOL SEPARAT LAB, BP 649, F-60206 COMPIEGNE, FRANCE

来源：

JOURNAL OF CHROMATOGRAPHY | 1993年 / 644卷 / 02期

关键词：

D O I：

10.1016/0021-9673(93)80711-G

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Catechol-2,3-dioxygenase (EC 1.13.11.2) from Pseudomonas putida as a model enzyme was purified from a bacterial crude extract in one step using affinity chromatography on immobilized histamine. In order to understand better the nature of the interaction, the adsorption of the enzyme on different gels having histidine and histamine coupled to Sepharose 4B was studied. The dissociation constants determined in the temperature range 4-37-degrees-C by an equilibrium binding analysis are between 0.95.10(-7) and 2.8.10(-7) M and between 2.6.10(-7) and 4.0.10(-7) M for histamine-carboxyhexyl Sepharose and histidyl-carboxyhexyl Sepharose, respectively. The standard enthalpy and entropy changes are different for these two gels, reflecting the different natures of the forces involved in the interaction.

引用

页码：289 / 297

页数：9

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