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Isolation, purification, and partial characterization of formate dehydrogenase from soybean seed
Authors:Farinelli M P  Fry D W  Richardson K E
Affiliation:The Ohio State University, Department of Physiological Chemistry, Columbus, Ohio 43210.
Abstract:Soybean (Glycine soja var Beeson) formate dehydrogenase has been isolated, purified, and partially characterized by affinity chromatography. The enzyme is a dimer having a total molecular weight of 100,000 and a subunit weight of 47,000. It has activity over a broad pH range, is stable for months at 4°C, and has Km values of 0.6 millimolar and 5.7 micromolar for formate and NAD, respectively.
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