Properties of a Protein Activator of NAD Kinase from Plants
作者： Shoshi Muto , Shigetoh Miyachi
DOI: 10.1104/PP.59.1.55
关键词:
摘要: Purification of pea ( Pisum sativum ) seedling NAD kinase by DEAE-cellulose column chromatography resulted in loss activity, due to dissociation an activator from the enzyme. The purified enzyme preparation, which was almost completely inactive, regained activity when added back. 320-fold ion exchange chromatographies. susceptible proteolytic enzymes, but not ribonuclease, glucoamylase or pectinase, indicating that it is a protein nature. This relatively stable boiling water, acid alkali, especially under high temperatures. Restoration catalytic inactive proportional amounts added. Gel filtration indicated molecular weight 28,000. found extracts various plants.
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