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Subcellular Localization of a UDP-Glucose:Aldehyde Cyanohydrin β-Glucosyl Transferase in Epidermal Plastids of Sorghum Leaf Blades
Author(s) -
Eve Syrkin Wurtele,
Susan S. Thayer,
Eric E. Conn
Publication year - 1982
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.70.6.1732
Subject(s) - triosephosphate isomerase , protoplast , plastid , biochemistry , biology , isomerase , phosphoenolpyruvate carboxykinase , transferase , phosphoenolpyruvate carboxylase , enzyme , chloroplast , gene
Epidermal and mesophyll protoplasts, prepared from leaf blades of 6-day-old light-grown Sorghum bicolor seedlings were separated by differential sedimentation and assayed for a number of enzymes. The epidermal protoplasts contained higher levels of NADPH-cytochrome c reductase (EC 1.6.2.4), triose phosphate isomerase (EC 5.3.1.1), phosphoenolpyruvate carboxylase (EC 4.1.1.31), and a UDP-glucose:cyanohydrin beta-glucosyl transferase (EC 2.4.1.85), but lower levels of NADP(+) triosephosphate dehydrogenase (EC 1.2.1.13) than did mesophyll protoplasts. When protoplast preparations were lysed and applied to linear sucrose density gradients, triosephosphate isomerase was found to be present in epidermal plastids. A significant fraction (41%) of the glucosyl transferase activity was also associated with the epidermal plastids.

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