Studies on cytochrome c peroxidase. I. Purification and some properties.
Studies on cytochrome c peroxidase. I. Purification and some properties.
复制标题
细胞色素c过氧化物酶的研究。
DOI：
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发表时间：
1965
影响因子：
4.8
通讯作者：
G. Ray
中科院分区：
文献类型：
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作者：
T. Yonetani;G. Ray
1940年，Altschul、Abrams和Hogness（1）在面包酵母中发现并纯化了细胞色素c过氧化物酶，可有效催化亚铁细胞色素c的过氧化氧化作用。两年后，同一作者（2）通过一种改进的方法获得了这种酶的高度纯化的制剂，该方法包括在甲苯存在下自溶，然后用水萃取，用硫酸铵和三氯乙酸沉淀，用乙醇分级，并在氢氧化铝上吸收。由于他们的纯化方法有些繁琐，产率相当低（约2a/ml），后来的工作者未能获得这种酶，其纯度不能达到最初工作者所达到的水平。因此，迄今为止发表的关于这种酶的所有后续研究都是用纯度较低的制剂进行的（3-11）。本文介绍了一种新的层析方法，从面包酵母中分离纯化细胞色素c过氧化物酶。本文介绍了纯化酶的一些性质。酶、H2 O2和亚铁细胞色素c之间的化学计量将在随附的论文（12）中描述。
Cytochrome c peroxidase, which effectively catalyzes the peroxidatic oxidation of ferrocytochrome c, was discovered in and purified from bakers’ yeast by Altschul, Abrams, and Hogness (1) in 1940. Two years later the same authors (2) obtained a highly purified preparation of this enzyme by an improved method which included autolysis in the presence of toluene followed by extraction with water, precipitation with ammonium sulfate and trichloroacetic acid, fractionation with ethanol, and absorption on aluminum hydroxide. Since their purification method was somewhat cumbersome and gave a rather poor yield (about 2a/,), subsequent workers have failed to obtain this enzyme in such a high purity as the original workers achieved. Thus all the subsequent studies on this enzyme so far published have been carried out with less pure preparations (3-11). The present paper describes the purification of cytochrome c peroxidase from bakers’ yeast by a new chromatographic method with a higher yield. Some properties of the purified enzyme are presented. The stoichiometry between the enzyme, H202, and ferrocytochrome c will be described in the accompanying paper (12).