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Effect of Oxidized Nucleotide Coenzymes and Mercaptoethanol on Stabilization of Plant Dehydrogenase Activity in Crude Extracts
Author(s) -
HAISSING BRUCE E.,
SCHIPPER ARTHUR L.
Publication year - 1975
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1975.tb03902.x
Subject(s) - cofactor , dehydrogenase , nucleotide , biochemistry , 2 mercaptoethanol , polyvinylpyrrolidone , chemistry , glyceraldehyde 3 phosphate dehydrogenase , glyceraldehyde , phosphate , enzyme , chromatography , biology , organic chemistry , gene
Activity loss of 6‐phosphogluconate, glucose‐6‐phosphate, and glyceraldehyde‐3‐phosphate dehydrogenases occurs in crude plant extracts prepared with insoluble polyvinylpyrrolidone (PVP) and a reducing agent, such as mercaptoethanol. Oxidized nucleotide coenzymes (1 m M ), in addition to mercaptoethanol (100 m M ), in the extraction buffer stabilizes activity of these dehydrogenases in extracts from both woody and herbaceous plants. PVP and mercaptoethanol alone equally stabilize malate dehydrogenase from most species tested. The mercaptoethanol and coenzyme treatment has proven useful in quantification, purification, and characterization of dehydrogenases in physiological investigations.