COPPER ENZYMES IN ISOLATED CHLOROPLASTS - POLYPHENOLOXIDASE IN BETA-VULGARIS
COPPER ENZYMES IN ISOLATED CHLOROPLASTS - POLYPHENOLOXIDASE IN BETA-VULGARIS
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DOI：
10.1104/pp.24.1.1
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发表时间：
1949-01-01
期刊：
影响因子：
7.4
通讯作者：
ARNON, DI
中科院分区：
文献类型：
--
作者：
ARNON, DI
菠菜甜菜（甜菜）的绿色叶提取物通过高速离心分离成叶绿体片段的悬浮液和几乎不含叶绿素的"细胞质液"。采用催化活性炭法测定了2个组分的多酚氧化酶活性。邻苯二酚与抗坏血酸为底物，并被发现定位在叶绿体悬浮液。在叶绿体悬浮液中的多酚氧化酶的本地化被证实，通过使用几个变种在操纵技术：在不同的pH值，进一步解体的叶绿体片段，叶绿体片段的提取，并添加到叶醪的粗马铃薯多酚氧化酶。与铜蛋白质性质的酶，其活性在叶绿体中被抑制氰化物，钠二乙基二硫代氨基甲酸盐和CO。CO的抑制不逆转光。
A green leaf extract of spinach beet (chard) was fractionated by highspeed centrifugation into a suspension of chloroplast fragments and a "cytoplasmic fluid" practically free of chlorophyll. Polyphenoloxidase activity of the 2 fractions was tested by using catalytic amts. of catechol with ascorbic acid as substrate, and was found to be localized in the chloroplast suspension. The localization of polyphenoloxidase in the chloroplast suspension was confirmed by using several variants in manipulative technique: extraction of chloroplast fragments at a different pH, further disintegration of the chloroplast fragments, and the addition of a crude potato polyphenoloxidase to the leaf mash. Consistent with the copper-protein nature of the enzyme, its activity in the chloroplasts was inhibited by cyanide, Na diethyldithiocarbamate and CO. The inhibition by CO was not reversed by light.