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Pyruvate Orthophosphate Dikinase in Wheat Leaves
Author(s) -
Kazuko Aoyagi,
James A. Bassham
Publication year - 1983
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.73.3.853
Subject(s) - polyacrylamide gel electrophoresis , enzyme , protein subunit , western blot , gel electrophoresis , chemistry , antiserum , immunoprecipitation , biochemistry , sodium , sodium dodecyl sulfate , specific activity , biology , gene , antibody , organic chemistry , immunology
Pyruvate orthophosphate dikinase (PPDK) was found in wheat (Triticum aestivum L. cv Cheyenne [CI 8885]) leaves both by activity assays and by the protein blot method. The specific activity of the wheat enzyme is comparable to that of PPDK from maize leaves. Of the total soluble protein in wheat leaves, about 0.05% was PPDK, comparable to the amount in the immature wheat seed and about 1/70th the amount found in mesophyll cells of maize. Immunoprecipitation of wheat PPDK with maize enzyme antiserum indicates partial identity, and the apparent subunit molecular weight is the same based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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