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Phosphorylation of glyoxysomal malate synthase from castor oil seed endosperm and cucumber cotyledon

Journal Article · · Plant Physiology, Supplement; (USA)
OSTI ID:6611070
;  [1]
  1. Univ. of Missouri, Columbia (USA)
Glyoxysomal malate synthase (MS) was purified to apparent homogeneity from 3-d germinating castor oil seed endosperm by a relatively simple procedure including two sucrose density gradient centrifugations. Antibodies raised to the caster oil seed MS crossreacted with MS from cucumber cotyledon. MS was phosphorylated in both tissues in an MgATP dependent reaction. The phosphorylation pattern was similar for both enzymes and both enzymes were inhibited by NaF, NaMo, (NH{sub 4})SO{sub 4}, glyoxylate and high concentration of MgCl{sub 2} (60 mM), but was not inhibited by NaCl and malate. Further characterization of the phosphorylation of MS from castor oil seed endosperms showed that the 5S form of MS is the form which is labelled by {sup 32}P. The addition of exogenous alkaline phosphatase to MS not only decreased enzyme activity, but could also dephosphorylate phospho-MS. The relationship between dephosphorylation of MS and the decrease of MS activity is currently under investigation.
OSTI ID:
6611070
Journal Information:
Plant Physiology, Supplement; (USA), Journal Name: Plant Physiology, Supplement; (USA) Vol. 89:4; ISSN PPYSA; ISSN 0079-2241
Country of Publication:
United States
Language:
English