反硝化假单胞菌细胞色素c过氧化物酶的分离与性质
Isolation and properties of cytochrome c peroxidase from Pseudomonas denitrificans.
作者信息
Coulson A F, Oliver R I
出版信息
Biochem J. 1979 Jul 1;181(1):159-69. doi: 10.1042/bj1810159.
Abstract
The isolation of cytochrome c peroxidase, cytochrome c4, cytochrome c-551 and azurin from Pseudomonas dentrificans is described. The peroxidase has a molecular weight of 63,000 and an isoelectric point of 5.6. Its absorption spectrum suggests that it contains two haem c groups/molecule. Preliminary steady-state kinetic data are reported with cytochromes c-551 and c4 and azurin as the second substrate.
摘要
描述了从反硝化假单胞菌中分离细胞色素c过氧化物酶、细胞色素c4、细胞色素c-551和天青蛋白的方法。该过氧化物酶的分子量为63,000，等电点为5.6。其吸收光谱表明每个分子含有两个血红素c基团。报道了以细胞色素c-551、细胞色素c4和天青蛋白作为第二底物的初步稳态动力学数据。
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