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Phosphodiesterase from cultured tobacco cells Physical and chemical properties

1977; Elsevier BV; Volume: 495; Issue: 1 Linguagem: Inglês

10.1016/0005-2795(77)90240-9

1878-1454

Hideaki Shinshi, Kunio Katō, Masanao Miwa, Taijiro Matsushima, Masao Noguchi, Takashi Sügimura,

Enzyme Catalysis and Immobilization

Phosphodiesterase isolated from suspension cultures of tobacco cells showed high affinity for concanavalin A-Sepharose and gave single superimposed bands of protein and carbohydrate on disc gel electrophoresis, suggesting that it is a glyco-protein. It contains 14% carbohydrate by weight, and has relatively high contents of basic and aromatic amino acids. Its isoelectric point is at pH 8.8, and the molecular weight of its subunits was estimated as 72 000 from a plot of the retardation coefficient on sodium dodecyl sulfate gel electrophoresis versus the molecular weight. The enzyme was catalytically active in an immobilized state on a concanavalin A-Sepharose column.