Unité Mixte Centre National de la Recherche Scientifique/Rhône-Poulenc (Unité Associée au Centre National de la Recherche Scientifique, U.M. 41), Rhône-Poulenc Agrochimie, 14-20 impasse Pierre Baizet, 69263 Lyon Cedex 09, France.
Plant Physiol. 1992 Mar;98(3):927-35. doi: 10.1104/pp.98.3.927.
The subcellular localization of O-acetyiserine(thiol)lyase (EC 4.2.99.8) in nongreen tissue from higher plants has been studied using purified proplastids, mitochondria, and protoplasts from cauliflower (Brassica oleracea L.) buds as a source of subcellular fractions. O-Acetylserine(thiol)lyase has been detected in both organelles (proplastids and mitochondria) and a cytosolic extract obtained by protoplast fractionation. We confirmed these observations, demonstrating that a form of the enzyme different in global charge and separated from others by anion-exchange chromatography corresponded to each subcellular location. Our observations are consistent with the need for cysteine biosynthesis in each subcellular compartment where the synthesis of proteins occurs.
已使用纯化的原质体、线粒体和花椰菜（ Brassica oleracea L.）芽原生质体作为亚细胞级分的来源，研究了高等植物非绿色组织中 O-乙酰丝氨酸（硫醇）裂解酶（EC 4.2.99.8）的亚细胞定位。在细胞器（原质体和线粒体）和通过原生质体分级分离获得的胞质提取物中均检测到 O-乙酰丝氨酸（硫醇）裂解酶。我们证实了这些观察结果，表明酶的一种形式在整体电荷上不同，并通过阴离子交换层析与其他形式分离，与每个亚细胞位置相对应。我们的观察结果与在发生蛋白质合成的每个亚细胞隔室中都需要半胱氨酸生物合成的观点一致。
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