지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
오류제보하기
We have partially purified S-adenosylmethionine decarboxylase (EC 4.1.1.50, SAMDC) from carnation (Dianthus caryophyllus L.) petals and generated polyclonal antibodies against CSDC 16 protein (Lee et al., 1996) overexpressed in E. coli. The protein has been puified approximately 126.8 fold through the steps involving ammonium sulfate fractionation, DEAE-Sepharose column chromatography and Sephacryl S-300 gel filtration. Its molecular mass was 42 kDa in native form and we could also detected a band of 32 kDa molecular mass on SDS-PAGE in western blot analysis using the polyclonal antibodies. The Km value of this enzyme for S-adenosylmethionine was 26.3$\mu$M. The optimum termperature and pH for S-adenosylmethionine decarboxylase activity were 35$^{\circ}C$ and pH 8.0, respectively. Putrescine and Mg2+ had no effects on hte activation of the enzyme activity. Mg2+ did not have any significant effects on the enzyme activity. SAMDC activity was inhibited by putrescine, spermidine and spermine. Methylglyoxal bis-(guanylhydrazone) (MGBG), carbonyl reagents such as hydroxylamine and phenylhydrazine, and sulfhydryl reagent such as 5, 5'-dithio-bis (2-nitrobenzoic acid) (DTNB) were effective inhibitors of the enzyme. However, isonicotinic acid hydrazide known as an inhibitor of 5'-pyridoxal phosphate (PLP) dependent enzyme activity had no significant effect on the enzyme activity. These results and our previously reported results (Lee et al., 1997b) suggest that S-adenosylmethionine decarboxylase is a heterodimer, $\alpha$$\beta$, and some carbonyl group and sulfhydryl group are involved in the catalytic activity.
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Studies on the regulation of Carnation S-adenosylmethionine decarboxylase during petal development.
한국동물학회 학술대회
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