{"title":"Purification of several NADP-dependent malate dehydrogenase isozymes from spinach leaves. Kinetic properties","authors":"Nathalie Ferté, Jean-Claude Meunier","doi":"10.1016/0304-4211(84)90213-X","DOIUrl":null,"url":null,"abstract":"<div><p>Four NADP-malate dehydrogenase (NADP-MDH) (EC 1.1.1.82) isozymes from spinach leaves have been purified to apparent homogeneity by DEAE-cellulose and affinity chromatography, and molecular sieving. They have the same native molecular weight (≈57 000) as determined by sedimentation equilibration analysis. They can be distinguished by their eletrocphoretic and chromatographic (over DEAE-cellulose) behaviors. On this basis, they constitute two sets of two enzymes each: MDH-A and -B, and MDH-C and -D. Catalytic properties of the most abundant isozyme, MDH-A, have been studied. Both NADPH and oxaloacetate inhibit the forward reductive reaction. Other kinetic parameters are also presented.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1984-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90213-X","citationCount":"6","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Science Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/030442118490213X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6
Abstract
Four NADP-malate dehydrogenase (NADP-MDH) (EC 1.1.1.82) isozymes from spinach leaves have been purified to apparent homogeneity by DEAE-cellulose and affinity chromatography, and molecular sieving. They have the same native molecular weight (≈57 000) as determined by sedimentation equilibration analysis. They can be distinguished by their eletrocphoretic and chromatographic (over DEAE-cellulose) behaviors. On this basis, they constitute two sets of two enzymes each: MDH-A and -B, and MDH-C and -D. Catalytic properties of the most abundant isozyme, MDH-A, have been studied. Both NADPH and oxaloacetate inhibit the forward reductive reaction. Other kinetic parameters are also presented.
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