• Bulletin of the Korean Chemical Society
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• 제25권2호
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• pp.165-166
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• 2004

• 한국환경생물학회:학술대회논문집
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• 한국환경생물학회 2001년도 학술대회
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• pp.113-114
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• 2001

• 한국발생생물학회:학술대회논문집
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• 한국발생생물학회 2001년도 전기 제11차 학술대회 논문집
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• pp.43-45
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• 2001

• 한국식물학회:학술대회논문집
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• 한국식물학회 2001년도 춘계학술발표대회:발표눈문요지록
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• pp.27-27
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• 2001

• 한국환경성돌연변이발암원학회:학술대회논문집
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• 한국환경성돌연변이발암원학회 2002년도 Current Trends in Toxicological Sciences
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• pp.92-92
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• 2002

• Bulletin of the Korean Chemical Society
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• 제25권2호
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• pp.249-252
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• 2004

Cytochrome P450 (P450)/$O_2$/NADPH engender electron transfer reaction of N-benzyl-N-substituted benzylamines to yield corresponding radical cation 1 that is simultaneously converted into 2 and 3. Subsequently, expulsion of proton and hydroxylation yielding a-hydroxylamines are followed by formation of benzaldehydes and benzylamines.

• 약학회지
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• 제39권4호
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• pp.450-460
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• 1995

The acute toxicity of fthalide in rat was studied in vivo by the observations of the changes in hematogram, serological parameters, content of cytochrome p-450, activities of NADPH-cytochrom c reductase, glucose-6-phosphatase, and the contents of cholinesterase and carboxylesterase in liver. Fthabde is a practically non-toxic substance(LD50 is 3.86g/kg), but rats were intoxicated with fthabde at a oral dose of 100 mg/kg for 12 days. WBC were significantly decreased and activities of ALT and LDH, on the cotrary, the content of glucose in serum were slightly increased. Cytochrome p-450 and lipid peroxide in liver were significantly increased in the fthalide-intoxicated rats. The longer administration of fthalide showed further increase of carboxylesterase activity in liver and serum, but decrease of activities of glucose-6-phosphatase and cholinesterase in liver and serum. These results show that fthatide can induce the hepatocellular injury and neurotoxicity.

• 한국독성학회:학술대회논문집
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• 한국독성학회 2002년도 Current Trends in Toxicological Sciences
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• pp.92-92
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• 2002

Recently we have reported that various hydroxystilbenes show strong inhibition of human P450 1 activity. A series of synthetic trans-stilbene derivatives were prepared and their inhibitory potentials were evaluated with the bacterial membrane of recombinant human P450 1A1, 1A2 or 1B1 coexpressed with human P450/NADPH-450 reductase to find new candidates for cancer chemoprevention.(omitted)

• 생명과학회지
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• 제19권8호
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• pp.1039-1046
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• 2009

다양한 천연물의 합성대사에 관여하는 식물 cytochrome P450 (P450s)은 그 기능적 다양성에도 불구하고, 이들 효소의 광범위한 기질 특이성을 설명해 줄 수 있는 구조분석에 대해서는 충분한 연구가 이루어지지 못하고 있는 실정이다. 식물 p-coumarate 3-hydroxylase (C3H)에 의해 매개되는 효소 반응은 lignin 과 다양한 phenylpropanoid 부산물들의 생합성에 매우 중요한 것으로 여겨지지만, 막 단백질인 C3H의 발현 및 정제가 효과적으로 이루어지지 못하여, 활성을 측정하기 위한 분석방법이 체계화 되지 못하고 있다. C3H의 작용기작과 기질특이성에 대해 폭넓은 이해를 위한 구조분석의 선행단계는 활성을 갖는 C3H를 밀리그램 단위로 분리, 정제하는 실험적 방법을 확립하는 것이라 할 수 있다. 이를 위해, 본 연구에서는 다양한 돌연변이 방법을 도입하여 식물 막단백질 C3H를 대장균 시스템에서 효과적으로 발현 및 정제할 수 있는 시스템을 사용하였다. 변형된 cytochrome P450 C3H ($C3H_{mod}$)을 세포막으로부터 고농도의 염완충용액을 이용하여 계면활성제 없이 추출하였으며, 2단계 chromatography를 통해 활성을 유지한 상태로 분리할 수 있었다. 이러한 실험적 기법은 NMR 및 X-ray crystallography와 같은 구조분석을 통한 C3H의 효과적인 분석에 적용될 수 있을 것이며, 또한 다른 식물 cytochrome P450 단백질의 효과적인 분석에도 적용 될 수 있을 것이다.

• Journal of Microbiology and Biotechnology
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• 제11권6호
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• pp.1011-1017
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• 2001

Streptomyces sp. Y-110 cytochrome P-450, induced by the addition of compactin -Na into the culture medium, was purified from the cell extract to apparent homogeniety, mainly by DEAE-Sepharose, hydroxyapatite, and Mono Q column chromatyography. The sepcific activity of purified enzyme on its substrate, compactin-Na, was determined to be 15 nmol of pravastatin per mg protein. The molecular mass of this enzyme on SDS-PAGE was $37{\pm}0.5$ kDa, pI was 4.5, and its CO difference spectrum showed maximum absorption peaks at 452 and 550nm, respectively. The N-terminal amino acid sequence was determined to be Met>Thr>Cys>Thr>Pro>Val>Thr>Val>The>Gly>Ala>Ala>Gly>Gln>Ile>Gly>Tyr>Ala>Leu. Its apparent $K_m$ on compactin-Na was $1.294{\mu}M{\cdot}min^-1,\;and\;V_{max}\;was\;1.028{\mu}M{\cdot}min^-1$. The maximum substrate concentration ($K_s$) for reaction was $270 {\mu}M$and thus $1/[K_s]$ was $3.7{\mu}M$. These physicochemical characteristics and kinetic behavior of this enzyme were compared and shown to be different from those of Streptomyces cytochrome P-450 enzymes reported, suggesting that this enzyme may be an additional member of the Streptomyces cytochrome P-450 family.