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
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Prophenoloxidase (pro-PO) has been confirmed in the hemolymph of the last larval hemolymph of Agrius convolvuli and purified through Sephadex G-100 gel filtration, DE-52 anion exchange chromatography and anion exchange HPLC. For activation of the purified pro-PO, the pro-enzyme was treated with trypsin, chymotrypsin and cetylpyridium chloride (CPC). The enzyme activation by specific proteolysis was observed only in the sample treat-ed with CPC. In analysis for substrate specificity of the active PO, it revealed that dopamin, dopa and 4-methylcatechol showed sequential high activity for' the enzyme. In particular, dopamin had the highest reactivity with the enzyme than other substrates. When the enzyme was incubated with 5 mM dopamin, maximum activity was reached within 10 min. Also, the activity was increased above $30^{\circ}C$ and it showed maximum activity at $70^{\circ}C$. Additionally, it was confirmed that the optimum pH for PO activity is 7.0.
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