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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 10, Number 6
BKCSDE 10(6)
June 20, 1989 

Catalytic Properties of Phospholipase D using Phosphatidic Acid as an Activator
Kwanyoung Jung, Eun-hie Koh, Myung-Un Choi*
The effects of phosphatidic acid(PA) on the activity of phospholipase D were examined in detail. The enzyme activity was examined in the liposome system containing phosphatidylcholine and PA, which was suspended in a desired buffer solution by ultrasonication. The substrate of large unilamella vesicle (LUV) state by ultrasonication was more effective on the enzyme activity than that of multilamella vesicle(MLV) by water-bath type sonication. The most effective molar ratio of PC-PA liposome for enzyme activity was found to be 1:0.7. The other optimum conditions were found 5 mM Ca2+ ion, pH 6.6, and incubation temperature of 27℃. Km and Vmax values were estimated to be 1.43 mM and 0.8 nmole/min/μg protein respectively. These properties in a PC-PA liposome system were compared with those in a PC-SDS mixed micelle system. The effects of other phospholipids and organic phosphates on the enzyme activity were also examined.
595 - 600
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