On the nature of chromophore in pig kidney diamine oxidase.

On the nature of chromophore in pig kidney diamine oxidase.
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猪肾二胺氧化酶发色团的性质。

DOI:
10.1111/j.1432-1033.1977.tb11409.x
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发表时间:
1977
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
B. Mondovì
B. Mondovì
中科院分区:
--
文献类型:
--
作者:
A. Agrò;P. Guerrieri;M. Costa;B. Mondovì

文献摘要

被引文献

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本文用吸收光谱法和荧光光谱法研究了猪肾二胺氧化酶中500 nm发色团的性质。从光谱测量可以得出以下结论。首先,500 nm吸收带不是由于铜,铜的减少与该带的消失无关。第二,苯肼和环丝氨酸与酶反应后,产生与吡哆醛酶天冬氨酸氨基转移酶非常相似的酶解。第三,这些酶衍生物出乎意料地是非荧光的。铜的去除,在还原剂和螯合剂的存在下的环丝氨酸处理的酶的长时间孵育后获得,导致类似于环丝氨酸-天冬氨酸转氨酶的荧光。有人提出,铜是协调的假定磷酸吡哆醛二胺氧化酶通过吡啶氮。
The nature of the 500-nm chromophore in pig kidney diamine oxidase was investigated by absorption spectroscopy and fluorescence in the presence of various chelating or carbonyl-specific reagents. From the spectroscopic measurements the following conclusions can be drawn. First, the 500-nm absorption band is not due to copper, the reduction of which is not related to the disappearance of this band. Second, phenylhydrazine and cycloserine give rise, upon reaction with the enzyme, to absorptions very similar to those of a pyridoxal enzyme, aspartate aminotransferase. Third, these enzyme derivatives are unexpectedly non-fluorescent. Copper removal, obtained after prolonged incubation of cycloserine-treated enzyme in the presence of reducing and chelating agents, leads to a fluorescence similar to that of cycloserine-aspartate transminase. It is proposed that copper is coordinated to the postulated pyridoxal phosphate of diamine oxidase through the pyridine nitrogen.