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J. Biochem, 1978, Vol. 83, No. 3 677-680
© 1978 Japanese Biochemical Society

research-article

Enzymatic Determination of Phospholipase D Activity with Choline Oxidase

Shigeyuki IMAMURA and Yoshifumi HORIUTI

Research Laboratory, Toyo Jozo Co., Ltd., Ohito-cho Tagata-gun, Shizuoka 410–23

A new enzymatic method was developed for the assay of phospholipase D [phosphatidylcholine phosphatidohydrolase EC 3.1.4.4 [EC] ] from cabbage leaves using choline oxidase from Arthrobacter globiformis cells. The method was based on the estimation of choline by the following series of enzymatic reactions after ending the phospholipase D reaction:


The amount of choline was proportional to the amount of resulting quinoneimine dye with an absorbance maximum at 500 nm. The phospholipase D reaction (choline liberation) was carried out at pH 5.5 in the presence of Ca2+ ions and ended by adding EDTA in conc. Tris-HCl buffer, pH 8, to give a final pH of around 8. The initial rate of the phospholipase D reaction was proportional to the enzyme concentration over the absorbance change range of 0 to 0.25 (equivalent to 0–21 µM of choline) under the optimal reaction conditions.


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