• Journal of Environmental Science International
• /
• v.7 no.1
• /
• pp.52-56
• /
• 1998

The effects of organophosphorus and carbamate pesticides were examined inhibition of the acetylcholinesterase activity in the chicken brain with enzyme-inhibition methods. The acetylcholinesterase activity in chicken brain determined by the Ellman method was 167 mmol/min/g protein. The optimum pH of acetycholinesterase was 8.2. $pl_{50}$ of acetycholinesterase by some organophosphorus were 3.80M of phosphorodlthioate, 4.04M of phosphorothioate, 6.33M of phosphate, and 6.60M of phosphrothiolate. pluto of acetycholinesterase by some carbamates were 5.1 OM of XMC, 5. 90M of carbofuran, 6.16M of isoprocarb, 6.30M of carbaryl, 6.47M of BPMC, and 6.77M of propoxur. pluto of carbamates selected was similar to that of phosphorothioate and phosphate organophosphates.

• The Korean Journal of Food And Nutrition
• /
• v.8 no.2
• /
• pp.79-87
• /
• 1995

It is generally known that the protein of talk has allergenicity and the allerenicity Induces allergic diseases. Finding methods to reduce the allergenicity of the food and develop methods to make low allergic food is the purpose of this study. For this study, 1 tried various experimental methods : heat treatment, irradation with ultraviolet and microwaves treatment with polyphosphate, enzyme hydrolysis and PCA inhibition test using guinea pigs and degrees of hydrolysis. The results obtained are as follows. Heat treatment reduced allergenicity of milk protein. The higher the heat, the better the effect. Irradiating with ultraviolet and microwave increased both the degree of protein hydrolysis and PCA inhibition reduced the allergenicity. Ultraviolet was more effective than microwaves on milk protein. Enzyme treatment increased the degree of hydrolysis and PCA inhibition, and reduced allergenicity considerably. Neutrase was more effective than alcalase on milk protein. Adding Polyphosphate did not induced protein hydrolysis, but increased PCA inhibition and reduced allergenicity.

• Food Industry
• /
• s.168
• /
• pp.28-31
• /
• 2002

한국산 콩 발효식품인 청국장과 된장의 생리활성효과에 대한 감마선의 영향을 살펴보았다. 청국장과 된장은 시중에서 구입하였으며 5,10,20 kGy의 선량으로 조사하였다. 생리활성효과로 angiotensin converting enzyme inhibition, xanthine oxidase inhibition, tyrosinase inhibition과 전자공여능을 살펴본 결과 10 kGy 보다 낮은 조사선량에서는 어떠한 영향도 끼치지 않는 것으로 나타났다.

• Journal of Plant Biology
• /
• v.33 no.4
• /
• pp.293-301
• /
• 1990

We have purified and characterized a deoxyribonuclease from zygotes of the eukaryotic green alga, Chlamydomonas reinhardtii and investigated effects of the polyamines, putrescine, spermidine and spermine on the purifed endonuclease-catalyzed cleavage of plasmid DNA. The enzyme has a molecular weight of about 37 kDa as measured by gel filtration and SDS-polyacrylamide gel electrophoresis. There is no requirement for a divalent cation. The activity is sensitive to ionic strength, as NaCl and KCl result in inhibition. The cleavage of plasmid DNA by the purified endonuclease was effectively inhibited by polyamines. The enzyme activity was inhibited more effectively by spermine than by spermidine. The inhibition by putrescine was lower than the other two polyamines.

• BMB Reports
• /
• v.33 no.1
• /
• pp.1-36
• /
• 2000

Acetohydroxyacid synthase (EC 4.1.3.18) catalyses the first reaction in the pathway for synthesis of the branched-chain amino acids. The enzyme is inhibited by several commercial herbicides and has been subjected to detailed study over the last 20 to 30 years. Here we review the progress that has been made in understanding its structure, regulation, mechanism, and inhibition.

• Applied Microscopy
• /
• v.17 no.2
• /
• pp.55-71
• /
• 1987

To investigate the effects of lead on the electron transport system and ultrastructure of mouse kidney mitochondria, various lead acetate concentrations were treated in vitro and respiration rate, enzyme activities were measured. Ultrastructural changes at state IV respiration were also observed. To compare with in vivo experiments, mouse were injected intraperitoneally of 100 mg lead acetate per kg body weight and state IV respiration rate and enzyme activities were measured. Ultrastructure of renal proximal tubular cells were also observed. In in vitro treatement, decreased state IV respiration, decreased enzyme activities, ruptured membranes and inhibition of condensed to orthodox transformation were observed. In in vivo treatment, decreased state IV respiration and decreased enzyme activities were observed after 24 hrs of i.p. injection. Cytochrome c oxidase activity showed twice the inhibition compared to NADH-CoQ reductase activity at 24 hrs. Continuous decreased state IV respiration was observed after 48 and 72 hrs of injection, however, the enzyme activities were increased to control level. Lead-protein complex which probably inhibits the toxic effects of lead appeared. To conclude, dominant effect of lead on the electron transport system appeared at cytochrome c oxidase activity, and the increased enzyme activities may be a result of appearance of lead-protein complex.

• BMB Reports
• /
• v.28 no.2
• /
• pp.100-106
• /
• 1995

S-adenosylmethionine (SAM) synthetase was purified to homogeneity from soybean (Glycine max) axes. The enzyme was purified 216-fold with a 1.5% yield by ammonium sulfate fractionation, acetone fractionation, ion exchange chromatography with DEAE-sephacel, gel filtration with Sephacryl S-300, and afffinity chromatography with ATP-agarose. The enzyme activity reached a maximum 3 days after germination. SAM synthetase had a subunit molecular weight of 57,000 daltons from a silver stained single band on SDS-PAGE. The molecular weight of the enzyme was 110,000 daltons from Sephacryl S-300 gel filtration. The enzyme was composed of two identical subunits. The $K_m$ values of the enzyme for L-methionine and ATP were 1.81 and 1.53 mM, respectively. The enzymatic activity was not affected by polyamines, agmatine, or SAM analogues, but was inhibited by SAM. The inhibition pattern was showed non-competitive for L-methionine and uncompetitive for ATP. The activity of SAM synthetase was inhibited by thiol-blocking reagents. The enzyme was induced by treatment with $10^{-3}$ M putrescine at germination. Experimental data revealed a possible novel regulation mechanism of polyamine biosynthesis through several endogenous intermediates.

• BMB Reports
• /
• v.36 no.2
• /
• pp.149-153
• /
• 2003

The dibucaine number (DN) was determined for serum cholinesterase (EC 3.1.1.8, SChE) in plasma samples. The ones with a DN of 79-82 were used, because they had the "usual" SChE variant. The enzyme was assayed colorimetrically by the reaction of 5,5'-dithiobis-[2-nitrobenzoic acid] (DTNB) with the free sulfhydryl groups of thiocholine that were produced by the enzyme reaction with butrylthiocholine (BuTch) or acetylthiocholine (AcTch) substrates, and measured at 412 nm. Dibucaine, a quaternary ammonium compound, inhibited SChE to a minimum within 2 min in a reversible manner. The inhibition was very potent. It had an $IC_{50}$ of $5.3\;{\mu}M$ with BuTch or $3.8\;{\mu}M$ with AcTch. The inhibition was competitive with respect to BuTch with a $K_i$ of $1.3\;{\mu}M$ and a linear-mixed type (competitive/noncompetitive) with respect to AcTch with inhibition constants, $K_i$ and $K_I$ of 0.66 and $2.5\;{\mu}M$, respectively. Dibucaine possesses a butoxy side chain that is similar to the butryl group of BuTch and longer by an ethylene group from AcTch. This may account for the difference in inhibition behavior. It may also suggest the existence of an additional binding site, other than the anionic binding site, and of a hydrophobic nature.

• The Journal of Internal Korean Medicine
• /
• v.19 no.1
• /
• pp.431-441
• /
• 1998

This study was undertaken to determine whether Buthus exract(BTE) affects Na^+-K^+-ATPase$ activity of nervous tissues. The enzym activity was measured in synaptosomal fraction prepared from rabbit brain cortex. Na^+-K^+-ATPase$ activity was inhibited by BTE over concentration range of 0.05-0.5% in a dose-dependent manner. The enzyme activity was increased by an increase in $Na^+$ concentration from 5 to 100mM, $K^+$ concentration from 0.5 to 10mM, and $Mg^{2+}$ concentration from 0.2 to 5mM. These changes in ion concentrations did not produce any effect on the inhibitory effect of BTE on $Na^+-K^+-ATPase$ activity. An increase in ATP concentration from 0.1 to 3mM caused an increase in the enzyme activity. The inhibition of the enzyme activity by BTE were not different between two ATP concentrations. A sulfhydryl group protector DTT prevented PCMB-induced inhibition of $Na^+-K^+-ATPase$ activity, but the BTE-induced inhibition was not altered by DTT. The inhibition of enzyme activity by combination of ouabain and BTE was not different from that by Buthus alone. These results suggest that Buthus exerts inhibitory effect on $Na^+-K^+-ATPase$ activity in cerebral synaptosomes, and the action mechansim is similar to that of ouabain.

• The Journal of Korean Institute for Practical Engineering Education
• /
• v.2 no.1
• /
• pp.35-41
• /
• 2010

An enzyme-catalized reaction is usually characterized by a very large increase in the rate and high specificity. Kinetics of simple enzyme-catalized reactions are often referred to as Michelis-Menten kinetics. A chemical that interferes with an enzyme's activity is called inhibitor. There are two types of enzyme inhibitions (viz. reversible and irreversible). If an inhibitor attaches to the enzyme with weak bonds, such as hydrogen bonds, the inhibition is usually reversible. Many enzyme reactions are also inhibited reversibly by their corresponding products. The rate of substrate disappearance together with the rate of product formation may be written by nonlinear differential equations. In the present study, numerical analyses of simple enzyme kinetics and inhibited enzyme kinetics are reported for the purpose of undergraduate education in engineering.