Contrasting Sensitivities of Chlorella and Higher Plant Phosphofructokinases to Dilution
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概要
- 論文の詳細を見る
A partially purified preparation of phosphofructokinase from Chlorella pyrenoidosa became unstable upon dilution. At pH 7.7 and 2℃, enzyme activity remained relatively constant when the protein concentration was 12 mg/ml, but at 3 mg/ml almost all activity was lost after 95 min. Greater stability was afforded by lower pH, higher temperature, or the presence of fructose-1,6-P_2, ATP or P_i. Phosphofructokinases from the leaves of spinach, oat and lucerne did not show the instability characteristics of the Chlorella enzyme.
- 日本植物生理学会の論文
著者
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Latzko Erwin
Botanisches Institut der Universitdt
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Latzko Erwin
Botanisches Institut Der Universitat Schlofigarten
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Kelly Grahame
Botanisches Institut Der Universitat Schlofigarten :(present)department Of Biochemistry And Nutritio
関連論文
- Purification, Kinetic and Regulatory Properties of Phosphofructokinase from Chlorella pyrenoidosa
- Contrasting Sensitivities of Chlorella and Higher Plant Phosphofructokinases to Dilution