EPIGENETIC INTERCONVERSIONS OF MULTIPLE FORMS OF MOUSE LIVER CATALASE
EPIGENETIC INTERCONVERSIONS OF MULTIPLE FORMS OF MOUSE LIVER CATALASE
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DOI：
10.1016/0014-5793(70)80488-4
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发表时间：
1970-01-01
期刊：
影响因子：
3.5
通讯作者：
MASTERS, CJ
中科院分区：
文献类型：
--
作者：
HOLMES, RS;MASTERS, CJ
虽然哺乳动物过氧化氢酶（过氧化氢：过氧化氢氧化还原酶，EC 1）的性质。11. 1.6)已被广泛研究，在目前的文献中，关于这种酶的多样性的程度和性质，意见分歧仍然很明显。从哺乳动物肝脏和红细胞提取物中分离出不同数量的过氧化氢酶异型物，研究人员使用聚丙烯酰胺[1,21]和淀粉凝胶电泳[3,4]、免疫电泳[5,61]和离子交换色谱[1,5,7 -91]等技术。此外，过氧化氢酶活性已在肝脏和肾脏的细胞汁液和颗粒组分中被确定，颗粒活性的主要部分定位于过氧化物酶体，可溶形式和结合形式（评论见[4，IO]）。电泳上不同的过氧化氢酶已经在这些单独的组分[3]和不同的组织中被鉴定出来[4,6]，这些组织来自大鼠和小鼠等物种；而其他哺乳动物，如绵羊和肉牛[1 1]在不同的组成组织和细胞下组分中表现出多种形式的统一模式。过氧化氢酶的这种复杂的多样性与酶的简单化学和遗传图谱形成鲜明对比。对牛肝过氧化氢酶的化学研究表明，该酶由四个相同的亚基组成[121]，利用人类和小鼠的先天性错误“过氧化氢血症”进行的遗传学研究表明，一个单一的结构基因负责酶的总合成（回顾见[131]）。本通讯试图调和这些明显不同的方面，提供evi-
Although the properties of mammalian catalase (hydrogen peroxide: hydrogen peroxide oxidoreductase, EC 1. 11. 1.6) have been extensively investigated, a diversity of opinion remains evident in the current literature as to the extent and nature of the multiplicity of this enzyme. Differing numbers of catalase heteromorphs have been resolved from mammalian liver and erythrocyte extracts by groups of workers using techniques such as polyacrylamide[1, 21 and starch gel electrophoresis [3, 4], immunoelectrophoresis[S, 61, and ion-exchange chromatography[1, 5, 7-91. In addition, catalase activities have been identified in both the cell sap and particmate fractions of liver and kidney with the major portion of the particulate activity being localized in the peroxisomes as both soluble and bound forms (for reviews see [4, IO]). Electrophoretically distinct catalases have been identified both in these separate fractions [3] and in different tissues [4, 6] from species such as rat and mouse; whereas other mammals such as sheep [4] and beef cattle [1 l] exhibit a uniform pattern of multiple forms throughout the different constituent tissues and subcelhrlar fractions. This complex multiplicity of catalase stands in contrast to the simple chemical and genetic picture of the enzyme. Chemical studies on beef liver catalase have shown that the enzyme consists of four identical subunits [121, and genetic studies, utilizing the inborn error “acatalasemia” in humans and mice, have indicated that a single structural gene is responsible for the total synthesis of the enzyme (for review see [131). This present communication attempts to reconcile these apparently divergent aspects by providing evi-