质体和叶绿体中丙酮酸激酶的同工酶。
Isoenzymes of pyruvate kinase in etioplasts and chloroplasts.
机构信息
Department of Biology, Queen's University, Kingston, Ontario K7L 3N6 Canada.
出版信息
Plant Physiol. 1979 May;63(5):903-7. doi: 10.1104/pp.63.5.903.
Abstract
Isoenzymes of pyruvate kinase from green leaves of castor bean and etiolated leaves of pea plants have been separated by ion filtration chromatography. One of the isoenzymes is localized in the plastid, whereas the other is in the cytosol. The cytosolic enzyme has a pH optimum from pH 7 to pH 9, and is able to utilize nucleotides other than ADP as the phosphoryl acceptor. The plastid enzyme has a much sharper optimum at pH 8, and is less efficient at using alternative nucleotides. The plastic pyruvate kinase, unlike the cytosolic enzyme, requires the presence of dithiothreitol or 2-mercaptoethanol during isolation and storage to stabilize the activity.
摘要
已通过离子过滤色谱法分离来自蓖麻绿叶和豌豆黄化叶片的丙酮酸激酶同工酶。同工酶之一位于质体中，而另一种位于细胞质溶胶中。胞质溶胶酶的 pH 最适范围为 pH 7 至 pH 9，并且能够利用除 ADP 以外的核苷酸作为磷酸受体。质体酶在 pH 8 时具有更尖锐的最佳 pH 值，并且使用替代核苷酸的效率较低。与胞质溶胶酶不同，质体丙酮酸激酶在分离和储存过程中需要二硫苏糖醇或 2-巯基乙醇的存在才能稳定其活性。
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