Purification and Characterization of Cytosolic 6-Phosphogluconate Dehydrogenase Isozymes from Maize
Author(s) -
Julia BaileySerres,
Minh T. Nguyen
Publication year - 1992
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.100.3.1580
Subject(s) - isozyme , dehydrogenase , biochemistry , cytosol , enzyme , substrate (aquarium) , biology , zea mays , chemistry , ecology , agronomy
Cytosolic isozymes of 6-phosphogluconate dehydrogenase were purified from roots of maize (Zea mays L.). The final preparation contained two 55-kD proteins. Affinity-purified dehydrogenases from a maize line that is null for both cytosolic 6-phosphogluconate dehydrogenase isozymes (Pgd1-null, Pgd2-null) lacked the 55-kD proteins. The substrate kinetics of the purified enzyme were determined.
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