• Journal of the Korean Chemical Society
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• v.47 no.5
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• pp.466-471
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• 2003

The effect of polyamines on the cabbage phospholipase D(PLD) activity was investigated. The PLD activity was determined by pH-stat titration of phosphatidic acid, one of the enzymatic reaction product, using phosphatidyl choline small unilamellar vesicles as a substrate. The cabbage PLD was activated approximately 4 fold by spermine at 1 mM concentration. This spermine effect appears to be similar to the previous report on the PLD activation of rat brain mitochondrial fraction. It was also found that cationic polypetides such as polylysine and polyhistidine exerted a marked enhancement effect on the cabbage PLD. Particularly polyhistidine exerted approximately 5.5 fold enhancement effect at 0.062 mM concentration. The polyamine effect on the cabbage PLD was reexamined in the phosphatidylcholine/sodium dodecyl sulfate mixed micellar system. The relevance of polyamine effect on PLD activity is discussed in relation to the active site of PLD.

• Journal of the Korean Chemical Society
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• v.31 no.1
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• pp.94-97
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• 1987

In a converting reaction of $p-bromo-\alpha-diethylaminoacetophenone$ (1a) and $p-bromo-\alpha-piperidinoacetophenone$ (1b) with KCN and $(NH_4)_2CO_3$, to hydantoin, the expected 5-(p-bromophenyl)-5-diethylaminomethylhydantion (2a) and 5-(p-bromophenyl)-5-piperidinomethylhydantoin (2b) were not formed. Diethylaminomethyl group and piperidinomethyl group were eliminated and p,p'-dibromodiphenylhydantil (4), which might be formed through dimerization of 5-(bromophenyl)-hydantoin (3), and p-bromobenzoic acid (5), which was formed through a degradation of 5-(bromophenyl)-hydantoin, were obtained. In the case of $p-bromo-\alpha-morpholinoacetophenone$ (1c), the expected 5-(p-bromophenyl)-5-morpholinomethylhydantoin (2c) was formed.