• Bulletin of the Korean Chemical Society
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• v.13 no.4
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• pp.381-384
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• 1992

The hydrolytic susceptibility of large unilamellar vesicle (LUV) toward cabbage phospholipase D (PLD) was studied. The activity of PLD was determined by pH stat titration method. Using phosphatidylcholine LUV as substrate a pH optimum of 6.96 was observed. For maximal activity the optimal temperature of $31^{\circ}C$ and 10 mM of Ca2+ were required. The apparent Km value estimated was 2.5 mM. The hydrolytic activity of PLD toward PC LUV was somewhat high despite the absence of activator in assay system and this high susceptibility of PC LUV may be attributed to the structural properties of LUV. The effect of amphiphatic substances such as dicetyl phosphate and phosphatidic acid on the enzyme activity were also examined in mixed LUVs.

• KSBB Journal
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• v.15 no.5
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• pp.497-500
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• 2000

Liposomes and proteoliposomes, artificial membranes, can interact with many solutes, such as drugs, peptides and proteins. The immobilization of (prot대)liposomes as supramolecular aggregates on gold surfaces have potential applications in nano and biosensor technology. We demonstrated a quartz crystal analyzer (QCA) based method to monitor the construction of multi-layers of unilamellar liposomes based on avidin-biotin binding on gold surfaces using a quartz crystal microbalance (QCM). Thus, the QCA provides an on line and efficient method of detecting the construction of protein membranes, which has applications in biosensing systems.