Modification of Maize Leaf Phosphoenolpyruvate Carboxylase with Fiuorescein Isothiocyanate : PROTEINS, ENZYMES AND METABOLISM

スポンサーリンク

概要

• 論文の詳細を見る

• Fluorescein isothiocyanate inactivates phosphoenolpyruvate carboxylase from maize leaves, presumably by reacting with lysyl groups. The reaction appears to involve at least two groups of lysines on the enzyme. The more rapid reaction is with groups which are protected by the substrate magnesium phosphoenolpyruvate and thus probably are located in the active site. In addition, fluorescein isothiocyanate apparently binds more slowly at a site which desensitizes the enzyme to activation by glucose-6-phosphate. Using the fluorescence of the complex of fluorescein isothiocyanate with phosphoenolpyruvate carboxylase it was shown that both magnesium phosphoenolpyruvate and glucose-6-phosphate cause changes in the conformation of the enzyme and influence the binding of fluorescein isothiocyanate as well. Light scattering measurements showed that fluorescein isothiocyanate induced desegregation of the enzyme, while glucose-6-phosphate caused aggregation, although less when fluorescein isothiocyanate was present.

• 日本植物生理学会の論文

著者

• Wu Min-xian

  Department Of Biochemistry University Of California

• Weddlng Randolph

  Department Of Biochemistry University Of California

関連論文

• Modification of Maize Leaf Phosphoenolpyruvate Carboxylase with Fiuorescein Isothiocyanate : PROTEINS, ENZYMES AND METABOLISM

スポンサーリンク