Laboratory of Chemical Biodynamics, University of California, Berkeley, California 94720.
Plant Physiol. 1983 Nov;73(3):853-4. doi: 10.1104/pp.73.3.853.
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.
在小麦(Triticum aestivum L. cv Cheyenne [CI 8885])叶片中发现了丙酮酸-5-磷酸二激酶(PPDK),通过活性测定和蛋白质印迹法都可以发现。该小麦酶的比活与玉米叶片的 PPDK 相当。在小麦叶片的总可溶性蛋白中,约有 0.05%是 PPDK,与未成熟小麦种子中的含量相当,约为玉米叶肉细胞中含量的 1/70。用玉米酶抗血清免疫沉淀小麦 PPDK 表明存在部分同源性,且根据十二烷基硫酸钠-聚丙烯酰胺凝胶电泳,其表观亚基分子量相同。