• Preventive Nutrition and Food Science
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• v.14 no.4
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• pp.358-361
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• 2009

Aldose reductase was purified to electrophoretic homogeneity from porcine liver. The purified enzyme was a monomer of 36 kDa. The enzyme was strongly inhibited by $Cu^{2+}\;and\;Mg^{2+}$ ions. Incubation of the enzyme with pyridoxal 5'-phosphate led to complete inhibition of enzymatic activity, suggesting that lysine residue is involved at or near the active site of the enzyme. The enzyme exhibited a broad substrate specificity. Furthermore, the enzyme was capable of decolorizing Alizarin, an anthraquinone dye.

• BMB Reports
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• v.31 no.5
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• pp.459-467
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• 1998

A new set of functional group interaction energy descriptors relevant to the ACE (Angiotensin-Converting Enzyme) inhibitory peptide, QSAR (Quantitative Structure Activity Relationships), is presented. The functional group interaction energies approximate the charged interactions and distances between functional groups in molecules. The effective energies of the computationally derived geometries are useful parameters for deriving 3D-QSAR models, especially in the absence of experimentally known active site conformation. ACE is a regulatory zinc protease in the renin-angiotensin system. Therapeutic inhibition of this enzyme has proven to be a very effective treatment for the management of hypertension. The non bond interaction energy values among functional groups of six-feature of ACE inhibitory peptides were used as descriptor terms and analyzed for multivariate correlation with ACE inhibition activity. The functional group interaction energy descriptors used in the regression analysis were obtained by a series of inhibitor structures derived from molecular mechanics and semi-empirical calculations. The descriptors calculated using electrostatic and steric fields from the precisely defined functional group were sufficient to explain the biological activity of inhibitor. Application of the descriptors to the inhibition of ACE indicates that the derived QSAR has good predicting ability and provides insight into the mechanism of enzyme inhibition. The method, functional group interaction energy analysis, is expected to be applicable to predict enzyme inhibitory activity of the rationally designed inhibitors.

• Applied Biological Chemistry
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• v.43 no.3
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• pp.174-178
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• 2000

To search CDK4/Cyclin D1 enzyme inhibition materials, methanol extracts of native eighty seven plant species in thirty seven families were screened in vitro for their inhibiting activities against CDK4/Cyclin D1 enzyme which are control to the normal cell division cycle in human body. Extracts of Paeonia suffruticosa, Saurus chinensis, Sanguisorba officinalis and Celastrus orbiculatus among them significantly inhibited above fifty percent $(in\;5\;{\mu}g/ml)$ against CDK4/ Cyclin D1 enzyme. Especially, the extracts of P. suffruticosa and S. officinalis showed moderately strong inhibition. Also, cryptotanshinone was identified as active compound from a extracts of Salvia mitiorrhiza by spectroscopic analyses including 2D NMR experiments.

• Journal of Acupuncture Research
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• v.18 no.2
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• pp.150-160
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• 2001

Objectives ; This study was undertaken to determine whether Carthami-Flos aquacapuncture (CFA) exerts protective effect against oxidant-induced inhibition of $Na^+-K^+$-ATPase activity in cerebral synaptosomes. Methods and Results ; The enzyme activity was dependent on incubation time and enzyme protein concentrations. An oxidant t-butylhydroperoxide (tBHP) at 1 mM concentration caused a significant inhibition of $Na^+-K^+$-ATPase activity, which was prevented by addition of 0.01% CFA. tBHP inhibition and CFA protection were independent on incubation time or enzyme protein concentrations. The enzyme activity was increased by ATP in a dose dependent manner. Effects of tBHP and CFA were not affected by ATP cocentrations. tBHP (1 mM) produced a significant increase in lipid peroxidation in cerebral synaptosomes, which was prevented by 0.01% CFA. CFA decreased oxygen free radicals generated induced by the phorbol-ester in a dose-dependent manner in human neutrophil. Conclusions ; These results suggest that CFA exerts protective effect against tBHP-induced inhibition of $Na^+-K^+$-ATPase activity, which is due to by an antioxidant action resulting from a direct scavenging effect of oxygen free radicals in the cerebral synaptosomes.

• Journal of Korean Society on Water Environment
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• v.26 no.4
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• pp.574-579
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• 2010

In this study the enzyme inhibition method using dehydrogenase which has been popularly used to estimate ecotoxicity was optimized. When three bacterial strains, Escherichia coli HB101, Enterobacter asburiae KCAD-4, and Aeromonas media KCAD-13, were compared, KCAD-4 was considered as the adequate strain to estimate toxicity because of its sensitivity and reproducibility. The optimal bacterial density was estimated as $5.4{\times}10^9CFU/mL$, at which the maximum sensitivity was observed. The phosphate buffer was suitable for the reaction solution. When the reaction times required for inhibition of enzyme activity by contact of toxicants and for reaction of damaged bacteria and substrate were tested, the optimal value was estimated as 20 min and 2 hrs, respectively. It is expected that the optimized conditions can be used to develop the standardized kits to estimate ecotoxicity of heavy metals in effluent from the industrial wastewater treatment facilities.

• Food Science and Biotechnology
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• v.18 no.2
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• pp.541-545
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• 2009

Water and ethanol extracts were prepared from the haesongi mushroom (Hypsizigus marmoreus) to measure functional components. The ability of the extracts to inhibit angiotensin-converting enzyme (ACE) and their hypoglycemic effects were also determined; the latter was measured by $\alpha$-amylase and glucosidase inhibition. Extraction yield, protein content, total phenol, and $\beta$-glucan in the water extracts were 55.86, 17.71, 1.89, and 21.93%, respectively. The respective values for the ethanol extracts were lower than those for water extracts. Both water and ethanol extracts showed dosedependent ACE inhibition, the effect of the former being greater. The water extract inhibited ACE activity by 95.34% at 40 mg/mL. The $IC_{50}$ values of the water extracts were 63.32 and 0.41 mg/mL for $\alpha$-amylase and glucosidase, respectively. Thus, the water extracts had a greater hypoglycemic effect than the ethanol extracts. From these results, water is a better solvent than ethanol to extract from the haesongi mushroom functional components that show ACE inhibition and have hypoglycemic effects.

• Archives of Pharmacal Research
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• v.14 no.4
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• pp.330-335
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• 1991

The effects of physostigmine and neostigmine on the parathin induced toxicity were examined in adult female rats. Physostigmine $(100\;{\mu}g/kg,\;ip)$ or neostigmine $(200\;{\mu}g/kg,\;ip)$ inhibited acetylcholinesterase (AChE) and cholinesterase (ChE) activities in blood, brain and lung when the enzyme activity was measured 30 min after the treatment. At the doses of two carbamates equipotent on brain AChE, neostigmine showed greater inhibition on peripheral AChE/ChE. The enzyme activity returned to normal in 120 min following the carbamates except in the lung of rats treated with neostigmine. Carbamates administered 30 min prior to parathion (2 mg/kg) antagonized the inhibition of AChE/ChE by parathion when the enzyme activity was measured 2 hr following parathion. Neostigmine showed greater protective effect on peripheral AChE/ChE. The effect of either carbamate on AChE/ChE was not significant 2 hr beyond the parathion treatment. Carbamates decreased the mortality of rats challenged with a lethal dose of parathion (4 mg/kg, ip) either when treated alone or in combination with atropine (10 mg/kg, ip). Lethal action of paraoxon (1.5 mg/ks ip), the active metabolite of parathion was also decreased by the carbamate treatment indicating that the protection was not mediated by competitive inhibition of metabolic conversion of parathion to paraoxon. The results suggest that carbamylation of the active sites may not be the sole underlying mechanism of protection provided by the carbamates.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.57-58
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• 2000

Production of dye-decolorizing enzyme was investigated with the cultivation of Geotrichum candidum Dec1 (abbreviated to Dec1) using molasses as a cheap raw materials. Molasses was found to stimulate the enzyme production as well as a role of carbon source, because the production increased with molasses content up to 50 g/L. However, the severe inhibition of dye-decolorizing enzyme activity was observed even at low concentration of molasses 10 g/L when purified decolorizing peroxidase was used. Its inhibitory effect was reduced through the cultivation of Dec1. The fractions of molasses separated by a gel chromatography showed the different degrees of inhibition. As a way to reduce the inhibitory effect, the dilution of culture broth was examined, and the total decolorizing activity for Reactive blue 5 increased 7 times as much as that of original culture broth by 30 times dilution. On the basis of result, we proposed a process scheme which can fully utilize both positive and negative effect of molasses in dye-decolorizing process using molasses.

• Journal of Integrative Natural Science
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• v.8 no.4
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• pp.267-272
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• 2015

Galactosemia is a potentially lethal disorder caused by the deficiency of the enzyme galactose-1-phosphate uridyltransferase (GALT) within the Leloir pathway. Galactokinase (GALK) is the enzyme in Leloir pathway which converts ${\alpha}$-D galactose to galactose 1-phosphate. The elevated level of galactose-1-phosphate, the product of GALK plays a major role in Galactosemia. Therefore the inhibition of GALK is a novel therapy for this disorder. Hence in the present study, we performed molecular docking of twenty inhibitors with different activity against galactokinase into the active site of galactokinase enzyme. The binding mode of these inhibitors was obtained using Surflex dock program interfaced in Sybyl-X2.0. The residues such as SER141, TYR109, ARG105, ARG228, TYR106, GLY346, GLY136, ASP86, ASP186 and SER142 found to interact with inhibitors.

• The Korean Journal of Food And Nutrition
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• v.9 no.2
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• pp.167-175
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• 1996

This studies were conducted to select optimal enzyme that produced hydrolysate from soybean, and to evaluated functionality of hydrolysate. Soybean powder was suspended with water and hydrolyzed by seven commercial proteases. Hydrolysate produced with protease from Bacillus subtilis showed the highest inhibition effect on the activity of angiotension converting enzyme(ACE), and the condition of enzymatic hydrolysis was 5cA substrate concentration, 0. l% enzyme concentration, 4 hour hydrolysis time. Under above optimum condition, soybean was hydrolyzed with protease from Bacillus subtilis yielding a DH (degree of hydrolysis) of about 49%. Hyrophobicity of hydrolysate was not correlated with the inhibition effect on ACE activity. The functionality of hydrolysate was significantly influenced by pH. Solubility of hydrolysate at alkali solution was greater than that at acidic solution.