• 한국식품영양과학회지
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• 제25권6호
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• pp.976-980
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• 1996

흰쥐를 대조군과 체중 100g 당 ethanol 0.3ml를 1일 1회 4일간 복강내로 투여한 실험군, 체중 100g당 toluene 0.3ml를 1일 1회 4일간 복강내로 투여한 실험군 및 ethanol 투여 2시간 후 toluene을 투여한 군으로 나누어 실험을 행하여 다음과 같은 결과를 얻었다. Alcohol 투여군, toluene투여군 모두 간 microsomal aniline hydroxylase(AH) 및 aminopyrine demethylase(AD) 활성도가 대조군 보다 유의한 증가를 보였다. Toluene과 ethanol의 병 행군은 toluene 투여군 보다 AH 및 AD 활성도가 다소 낮게 나타나는 경향을 보였다. 간조직 중 benzylalcohol dehydrogenase 활성도 역시 alcohol 및 toluene 투여군 모두 대조군에 비하여 높게 나타났으며 toluene과 alcoho의 병행투여군은 toluene 투여군 보다 본 효소 활성도가 다소 낮게 나타나는 경향을 보였다. 한편 간조직 중 benzaldehyde dehydrogenase 활성도는 alcohol 및 toluene 투여군 모두 대조군에 비하여 증가되는 경향을 보였으며 alcohol과 toluene의 병행투여군은 toluene 투여군 보다 유의한 감소를 보였다. 또한 간조직 중 xanthine oxidase 활성도는 alcohol과 toluene 병행 투여군이 toluene 투여군 보다 유의하게증가되었다. 이상 실험성적을 종합해 볼 때 alcohol의 전처치는 toluene 대사 효소 활성도를 억제시켜 toluene 대사에 영향을 미칠 것으로 생각된다.

• 한국환경보건학회지
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• 제19권3호
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• pp.58-63
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• 1993

In order to elucidate the alteration of drug-metabolizing enzymes and mechanism in the animal with hepatic injury and ketosis, the regulation of P450IIE was studied in the rats with heaptic injury caused by CCl$_4$ and with ketosis caused by streptozotocin and high-fat diet. P450IIE expression in liver was examined by the combination of enzyme activities, Western immunoblot, and mRNA Northern blot analyses using specific polyclonal antibody and cDNA probe for P450IIE. Enzyme activity and amounts of immunoreactive P450IIE were rapidly decreased in a time-dependent manner after a single dose of CCl$_4$ . However, the decreases in P450IIE enzyme activity and immunoreactive protein by CCl$_4$ were not accompanied by a decline in its mRNA level. The data thus suggested a post-translational reduction of P450IIE by CCl$_4$. The enzyme activities (aniline hydroxylase) in hepatic microsomes were elevated about 2-3-fold by streptozotocin and feeding with a high fat diet. This increases in enzyme activities were also accompanied by 3-fold increases in immunoreactive P450IIE protein and its mRNA. Our data thus indicated that P450IIE induction during the ketosis appears to be due to pretranslational activation.

• 대한약학회:학술대회논문집
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• 대한약학회 2000년도 NEW STRATEGY FOR DRUG DEVELOPMENT IN POST-GENOMIC ERA(대한약학회)
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• pp.237.3-238
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• 2000

• Archives of Pharmacal Research
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• 제3권2호
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• pp.79-84
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• 1980

Eight species of the genus Angelica in Korea were examined for the activity of affecting drug metabolism and for the presence of coumarins. The results showed that various parts, especially roots and fruits of Angelica plants had strong effects on drug metabolism and that they contained various derivatives of coumarins.

• 한국독성학회:학술대회논문집
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• 한국독성학회 2003년도 추계학술대회
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• pp.166-166
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• 2003

Cytochrome P-450 3A4 (CYP3A4) is major enzyme in human liver, the role of this is detoxification and metabolizing more than 50% clinical drugs in use. The transcription of CYP3A4 is regulated by the Pregnenolone X receptor (PXR),of which human form is Steroid and Xenobiotics receptor (SXR).(omitted)

• 한국영양학회:학술대회논문집
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• 한국영양학회 2001년도 춘계연합학술대회 초록
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• pp.306.2-306
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• 2001

• Journal of Microbiology and Biotechnology
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• 제34권6호
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• pp.1270-1275
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• 2024

Human gut bacterium Dorea sp. MRG-IFC3 is unique in that it is capable of metabolizing puerarin, an isoflavone C-glycoside, whereas it shows broad substrate glycosidase activity for the various flavonoid O-glycosides. To address the question on the substrate specificity, as well as biochemical characteristics, cell-free biotransformation of flavonoid glycosides was performed under various conditions. The results showed that there are two different enzyme systems responsible for the metabolism of flavonoid C-glycosides and O-glycosides in the MRG-IFC3 strain. The system responsible for the conversion of puerarin was inducible and comprised of two enzymes. One enzyme oxidizes puerarin to 3"-oxo-puerarin and the other enzyme converts 3"-oxo-puearin to daidzein. The second enzyme was only active toward 3"-oxo-puerarin. The activity of puerarin conversion to daidzein was enhanced in the presence of Mn²⁺ and NAD⁺. It was concluded that the puerarin C-deglycosylation by Dorea sp. MRG-IFC3 possibly adopts the same biochemical mechanism as the strain PUE, a species of Dorea longicatena.

• Archives of Pharmacal Research
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• 제7권1호
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• pp.53-56
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• 1984

The effect of twenty two spices on liver microsomal monooxygense activity was tested as measured by alteration of hexobarbital (HB) narcosis and strychnine mortality in mice. Oral administration of seven spices for 7 consecutive days caused a significant shortening of the duration of HB-induced sleeping time. The treatment of mice with a single i. p. injection of 9 spices resulted in a significant prolongation of the sleeping time. White pepper, dill and fennel reduced the toxicity of strychnine. These results strongly indicated that some spices might affect the activity of liver microsomal drug metabolizing enzyme (DME) function.

• Journal of Microbiology and Biotechnology
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• 제16권5호
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• pp.778-785
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• 2006

Catechol 1,2-dioxygenase was purified from cells of R. rhodochrous N75 grown at the expense of benzoate and p-toluate as the sole sources of carbon. A single catechol 1,2-dioxygenase was found to be induced with either growth substrate. The enzyme has an estimated $M_r$ of 71,000 consisting of two identical subunits. Catechol 1,2-dioxygenase from R. rhodochrous N75 exhibits some unusual properties including: broad substrate specificity, extradiol cleavage activity with 4-methylcatechol and low $K_m$ values for halocatechols, suggesting that this enzyme is distinct from other known catechol and chlorocatechol 1,2-dioxygenases.

• 생약학회지
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• 제25권1호
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• pp.47-50
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• 1994

For the biological survey, effects of Ailanthi Cortex Radicis, the root bark of Ailanthus altissima(Simaroubaceae) on epoxide hydrolyzing enzymes were checked. The methanolic extract and its chloroform fraction were shown to activate the liver metabolizing enzyme system including epoxide hydrolase system which was monitored by activities of transaminase, lactate dehydrogenase, alkaline phosphatase and epoxide hydrolase system in bromobenzene treated rats. But they showed no effect on glutathione S-transferase activity.