• Journal of Life Science
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• v.18 no.7
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• pp.1005-1010
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• 2008

In this study, we investigated the inhibitory effect of four solvent fractions of Alnus firma on ${\alpha}-amylase$, ${\alpha}-glucosidase$ and aldose reductase activities. The inhibitory test showed that methanol (MeOH) extract and hexane (HX) fraction strongly inhibited pork pancreatin and salivary ${\alpha}-amylase$ activity. The MeOH extract and HX fraction of Alnus firma at the concentration of 4 mg/ml inhibited more than 70% of pancreatin and salivary ${\alpha}-amylase$ activity. The inhibitory effect of fractions has different specificities against ${\alpha}-amylase$ from pancreatin and salivary. In addition, the MeOH extract and butanol (BuOH) fraction showed the highest inhibitory activity on yeast ${\alpha}-glucosidase$ at values of $IC_{50}$ $137.36\;{\mu}g/ml$ and $115.14\;{\mu}g/ml$ respectively. The MeOH extract and BuOH fraction showed the highest inhibitory activity on yeast ${\alpha}-glucosidase$ than commercial agent such as 1-deoxynorjirimycin and acarbose. Inhibition kinetics of solvent fractions showed that ${\alpha}-glucosidase$ has been inhibited noncompetitively by the MeOH, EA and BuOH fraction. The aldose reductase from human muscle cell had been inhibited strongly by the MeOH extract and EA fraction at 57.996% and 83.293% at the concentration of $50\;{\mu}g/ml$, respectively. These findings may contribute to biological significance in that ${\alpha}-amylase$, ${\alpha}-glucosidase$ and aldose reductase inhibitory compounds could be used as a functional food and a drug for the symptomatic treatment of antidiabetic disease in the future.

• BMB Reports
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• v.28 no.2
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• pp.118-123
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• 1995

Biodegradative threonine dehydratase was purified to homogeneity from Serratia marcescens ATCC 25419 by streptomycin sulfate treatment, Sephadex G-200 gel filtration chromatography followed by AMP-Sepharose 4B affinity chromatography. The molecular weight of the purified enzyme was 118,000 by fast protein liquid chromatography using superose 6-HR. The enzyme was determined to be a homotetrameric protein with subunit molecular weights of 30,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was inhibited by ${\alpha}-Keto$ acids and their derivatives such as ${\alpha}-ketobutyrate$, pyruvate, glyoxlyate, and phosphoenol pyruvate, but not by ${\alpha}-aminobutyrate$ and ${\alpha}-hydroxybutyrate$. The inhibition of the enzyme by pyruvate and glyoxylate was observed in the presence of AMP. The inhibitory effect of glyoxylate was decreased at high enzyme concentration, whereas the inhibition by pyruvate was independent of the enzyme concentration. The kinetics of inhibition of the enzyme by pyruvate and glyoxylate revealed a noncompetitive and mixed-type inhibition by the two inhibitors with respect to L-threonine and AMP, respectively.

• Journal of Photoscience
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• v.1 no.1
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• pp.47-52
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• 1994

Effects of HgCl$_2$-treatment on electron transport, chlorophyll a fluorescence and its quenching were studied using isolated barley (Hordeum vulgare L. cv. Albori) chloroplasts. Depending on the concentration of HgCI$_2$, photosynthetic oxygen-evolving activities of photosystem II (PS II) were greatly inhibited, whereas those of photosystem I (PS I) were slightly decreased. The inhibitory effects of HgCl$_2$ on the oxygen-evolving activity was partially restored by the addition of hydroxyamine, suggesting the primary inhibition site by HgCl$_2$2-treatment is close to the oxidizing site of PS tl associated with water-splitting complex. Addition of 50 $\mu$M HgCI$_2$ decreased both photochemical and nonphotochemical quenching of chlorophyll fluorescence. Especially, energy dependent quenching (qE) was completely disappeared by HgCl$_2$-treatment as observed by NH$_4$CI treatment. In the presence of HgCI$_2$, F'o level during illumination was also increased. These results suggest that pH gradient across thylakoid membrane can not be formed in the presence of 0 $\mu$M HgCl$_2$. In addition, antenna pigment composition might be altered by HgCl$_2$-treatment.

• Journal of Microbiology and Biotechnology
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• v.19 no.5
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• pp.447-454
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• 2009

The transport of spermidine into a cyanobacterium, Synechocystis sp. pec 6803, was characterized by measuring the uptake of $^{14}C$-spermidine. Spermidine transport was shown to be saturable with an apparent affinity constant ($K_m$) value of $67{\mu}M$ and a maximal velocity ($V_{max}$) value of 0.45 nmol/min/mg protein. Spermidine uptake was pH-dependent with the pH optimum being 8.0. The competition experiment showed strong inhibition of spermidine uptake by putrescine and spermine, whereas amino acids were hardly inhibitory. The inhibition kinetics of spermidine transport by putrescine and spermine was found to be noncompetitive with $K_i$ values of 292 and $432{\mu}M$, respectively. The inhibition of spermidine transport by various metabolic inhibitors and ionophores suggests that spermidine uptake is energy-dependent. The diminution of cell growth was observed in cells grown at a high concentration of NaCl. Addition of a low concentration of spermidine at 0.5 mM relieved growth inhibition by salt stress. Upshift of the external osmolality generated by either NaCl or sorbitol caused an increased spermidine transport with about 30-40% increase at 10 mosmol/kg upshift.

• Journal of Pharmacopuncture
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• v.19 no.1
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• pp.45-50
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• 2016

Objectives: The purpose of this study was to investigate the antifungal effect of bee venom (BV) and sweet bee venom (SBV) against Candida albicans (C. albicans) clinical isolates. Methods: In this study, BV and SBV were examined for antifungal activities against the Korean Collection for Type Cultures (KCTC) strain and 10 clinical isolates of C. albicans. The disk diffusion method was used to measure the antifungal activity and minimum inhibitory concentration (MIC) assays were performed by using a broth microdilution method. Also, a killing curve assay was conducted to investigate the kinetics of the anti-fungal action. Results: BV and SBV showed antifungal activity against 10 clinical isolates of C. albicans that were cultured from blood and the vagina by using disk diffusion method. The MIC values obtained for clinical isolates by using the broth microdilution method varied from $62.5{\mu}g/mL$ to $125{\mu}g/mL$ for BV and from $15.63{\mu}g/mL$ to $62.5{\mu}g/mL$ for SBV. In the killing-curve assay, SBV behaved as amphotericin B, which was used as positive control, did. The antifungal efficacy of SBV was much higher than that of BV. Conclusion: BV and SBV showed antifungal activity against C. albicans clinical strains that were isolated from blood and the vagina. Especially, SBV might be a candidate for a new antifungal agent against C. albicans clinical isolates.

• Proceedings of the PSK Conference
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• 2002.10a
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• pp.383.3-384
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• 2002

Rosmarinic acid (1) and methyl rosmarinic acid (2), isolated from the ethyl acetate soluble fraction of the methanolic extract of Salvia miltiorrhiza Bunge (Lamiaceae) were found to be the tyrosinase inhibitors and scavengers of 1, 1-diphenyl-2-picrylhydrzyl (DPPH) radical. Compounds 1 and 2 inhibited the oxidation of L-tyrosine catalyzed by mushroom tyrosinase with $IC_{50}$/ of 16.8 $\mu\textrm{M}$ and 21.5 $\mu\textrm{M}$. respectively. It compared well with kojic acid. a well-known tyrosinase inhibitor. with an $IC_{50}$ of 22.4 $\mu\textrm{M}$. The inhibitory kinetics, analyzed by a Lineweaver-Burk plot, found rosmarinic acid and its methyl ester to be competitive inhibitors with $K_{i}$ of $2.35{\times}10^{-5}M$ and $1.52{\times}10^{-5}M$ respectively. In addition, compounds 1 and 2 showed the scavenging activities on DPPH radical, with $IC_{50}$ of 4.27 $\mu\textrm{M}$ and 3.05 $\mu\textrm{M}$. respectively. These scavenging effects were more potent than that of L-ascorbic acid ($IC_{50}$ = 11.75$\mu\textrm{M}$).

• Proceedings of the Korean Society of Applied Pharmacology
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• 1998.11a
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• pp.171-171
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• 1998

The metabolic behavior of Debaryomyces hansenii was investigated in terms of substrate utilization and by product formation under different cultural conditions. Debaryomyces hansenii exhibited best growth and most tolerant of increased NaCl, sucrose and potassium sorbate at their optimum pH (5.0). A combination of two or more environmental stresses had stronger inhibitory effects on their growth kinetics, utilization of carbohydrate substrates and the production of organic acids, volatile compounds and other metabolites. Significant amounts of glycerol (0.35-4.4 g/L) and arabitol (0.08-9.8 g/L) were produced by D. hansenii. The main organic acids produced were citric (0.6-1.4 g/L), acetic (0.3-2.8 g/L), fumaric (0.2-1.0 g/L) and malic acids (1.1-1.7 g/L). A range of other compounds such as ethyl acetate, n-propanol, isoamyl alcohol, 2-phenylethanol and acetoin were also produced. The concentration of these compounds varied with the cultural conditions. Such compounds would have specific impacts on food quality in which D. hansenii is found.

• The Korean Journal of Physiology and Pharmacology
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• v.3 no.5
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• pp.461-469
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• 1999

Glutamate and ${\gamma}-aminobutyric$ acid (GABA) are major excitatory and inhibitory neurotransmitters in the vertebrate retina, respectively. Using the whole-cell patch clamp technique and a rapid solution changer, glutamate and GABA receptors have been extensively investigated in carp retina. Glutamate receptors on both horizontal and amacrine cells may be an AMPA preferring subtype, which predominantly consists of flop splice variants. $GABA_A$ and $GABA_C$ receptors coexist in bipolar cells and they both show significant desensitization. Kinetics analysis demonstrated that activation, deactivation and desensitization of the $GABA_C$ receptor-mediated response of these cells are overall slower than those of the $GABA_A$ response. Endogenous modulator $Zn^{2+}$ in the retina was found to differentially modulate the kinetic characteristics of the $GABA_C$ and $GABA_A$ responses.

• Journal of Microbiology and Biotechnology
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• v.15 no.3
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• pp.573-578
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• 2005

Pyrimidine nucleotide N-ribosidase (pyrimidine 5'-nucleotide phosphoribo(deoxyribo)hydrolase/pyrimidine 5'-nucleotide nucleosidase, EC 3.2.2.10) catalyzes the breakdown of pyrimidine 5'-nucleotide into pyrimidine base and ribose(deoxyribo)-5-phosphate. However, detailed characteristics of the enzyme have not yet been reported. The enzyme was purified to homogeneity 327.9-fold with an overall yield of $6.1\%$ from Pseudomonas oleovorans ATCC 8062. The enzyme catalyzed cytidine monophosphate (CMP) and uridine monophosphate (UMP), but not adenosine monophosphate (AMP) and guanosine monophosphate (GMP). The enzyme optimally metabolized CMP at pH 6.0 and UMP at around 8.5, and the optimum temperature for the overall enzyme reaction was found to be $37^{\circ}C$. The $K_m$ values of the enzyme for CMP (at pH 6.0) and UMP (at pH 8.5) were 1.6 mM and 1.1 mM, respectively. AMP, deoxyCMP, and deoxyUMP were very effective inhibitors of the reaction. Double-reciprocal plots obtained in the absence and in the presence of AMP revealed that this inhibitory effect was of the mixed competitive type with respect to the breakdown of CMP and of the noncompetitive type with respect to the breakdown of UMP. In the presence of AMP, the enzyme followed sigmoid kinetics with respect to each substrate.

• The Korean Journal of Physiology and Pharmacology
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• v.3 no.3
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• pp.305-313
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• 1999

To explore whether $Cl^-$ channel blockers interact with the ATP-sensitive $K^+\;(K_{ATP})$ channel, I have examined the effect of two common $Cl^-$ channel blockers on the $K_{ATP}$ channel activity in isolated rat ventricular myocytes using patch clamp techniques. In inside-out patches, 4,4'-diisothio-cyanatostilbene- 2,2'-disulfonic acid (DIDS) and niflumic acid applied to bath solution inhibited the $K_{ATP}$ channel activity in a concentration-dependent manner with $IC_{50}$ of 0.24 and 927 ${\mu}M,$ respectively. The inhibitory action of DIDS was irreversible whereas that of niflumic acid was reversible. Furthermore, DIDS-induced block was not recovered despite exposure to ATP (1 mM). In cell-attached and inside-out patches, DIDS blocked the pinacidil- or 2,4-dinitrophenol (DNP)-induced $K_{ATP}$ channel openings. In contrast, niflumic acid did not block the pinacidil-induced $K_{ATP}$ channel openings in inside-out patches, but inhibited it in cell-attached patches. DIDS and niflumic acid produced additional block in the presence of ATP and did not affect current-voltage relationship and channel kinetics. All these results indicate that DIDS among $Cl^-$ channel blockers specifically blocks the cardiac $K_{ATP}$ channel.