Julliard J H, Breton-Gilet A
Unité Mixte de Recherches 41 CNRS-Rhône-Poulenc Agrochimie, Centre deRecherches de la Dargoire, Lyon, France.
Protein Expr Purif. 1997 Feb;9(1):10-4. doi: 10.1006/prep.1996.0666.
Hydroxypyruvate reductase (HPR), a plant leaf peroxisomal enzyme involved in the glycolate pathway, has been purified in two steps from a crude extract of parsley leaves during the purification of an unrelated ATP-dependent enzyme. HPR, a homogenous side-fraction arising from this purification procedure, was identified after sequencing of three internal peptides which showed near 100% homology with the amino acid sequence deduced from the cDNA encoding the NADH-dependent HPR from cucumber. This is an example of the identification of the activity of an unknown protein through direct sequence work. Some of the parsley HPR physicochemical and kinetic properties are similar to those of the cucumber enzyme.
羟基丙酮酸还原酶（HPR）是一种参与乙醇酸途径的植物叶片过氧化物酶体酶，在纯化一种不相关的ATP依赖性酶的过程中，分两步从欧芹叶粗提物中纯化得到。HPR是该纯化过程中产生的一种均一的旁组分，在对三个内部肽段进行测序后得以鉴定，这些肽段与从编码黄瓜NADH依赖性HPR的cDNA推导的氨基酸序列显示出近100%的同源性。这是通过直接测序工作鉴定未知蛋白质活性的一个例子。欧芹HPR的一些物理化学和动力学性质与黄瓜酶的相似。
