• Parasites, Hosts and Diseases
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• 제21권1호
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• pp.41-48
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• 1983

The activity and distribution of aspartate aminotransferase (EC 2.6. 1. 1) and alanine aminotransferase (EC 2.6.1.2) in adult Fascicle hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1g of Fascicle hepatica, respectively. 2. The activity of those enzymes was relatively low compared with those in mammalian tissues. 3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71% of the activity was in cytosolic, 24% in mitochondrial and 5% was in nuclear fraction. 4. About 22% of the total alanine aminotransferase activity was found in the mitochondrial fratstion, about 66% in the cytosolic fraction. 5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.

• 전기화학회지
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• 제12권4호
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• pp.311-316
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• 2009

인공해수에서 일어나는 Al의 부식에 대하여 alanine과 methionine의 부식억제 효과를 조사하였다. 이들 아미노산의 낮은 덮힘율로 보아 Al 표면에 alanine과 methionine는 Langmuir adsorption isotherm에 따른 흡착이 일어나며, 아미노산 안의 카르복시 이온만이 Al에 흡착하는 것으로 보인다.

• Bulletin of the Korean Chemical Society
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• 제14권6호
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• pp.700-704
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• 1993

The photocatalytic alanine and hydrogen production reaction were studied by using CdS as a semiconductor photocatalysts. The rate of alanine and hydrogen production depends strongly on the temperature in heat treatment of CdS powder. In particular, the rate of alanine production, which was observed using Pt/CdS(A)-(CdS from Mitsuwa), was increased about six times than that of using Pt/CdS(B)-(CdS from Furruchi) under the same heat treatment condition at 500$^{\circ}$C. And the photocatalytic activity for alanine production using bare CdS(A) or Pt/CdS(A) was almost same with increasing temperature in heat treatment in the range of 100-600$^{\circ}$C. From X-ray diffraction data and photoluminescence spectrum, we conclude that the crystal structure changes of CdS(A) or strong interaction at interface of Pt and CdS contribute to increasing the rate of alanine and hydrogen production reaction.

• Nutritional Sciences
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• 제6권4호
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• pp.189-194
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• 2003

Most of the ethyl alcohol consumed by humans is oxidized to acetaldehyde in the liver by the cytoplasmic alcohol dehydrogenase (ADH) system. For this ADH-catalyzed oxidation of alcohol, $NAD^+$ is required as the coenzyme and $NAD^+$becomes reduced to NADH. As the $NAD^+$becomes depleted and NADH accumulates, alcohol oxidation is reduced. For continued alcohol oxidation, the accumulated NADH must be quickly reoxidized to $NAD^+$, and it is this reoxidation of NADH to $NAD^+$that is known to be the rate-limiting step in the overall oxidation rate of alcohol The reoxidation of NADH to $NAD^+$is catalyzed by lactate dehydrogenase in the cytoplasm of hepatocytes, with pyruvate being utilized as the substrate. The pyruvate may be supplied from alanine as a result of amino acid metabolism via the urea cycle. Also, glutamine is thought to help with the supply of pyruvate indirectly, and to activate the urea cycle by producing $NH_3$. Thus, in the present study, we have examined the effects of alanine and glutamine on the alcohol oxidation rate. We utilized isolated perfused liver tissue in a system where media containing alanine and glutamine was circulated. Our results showed that when alanine (5.0mM) was added to the glucose-free infusion media, the alcohol oxidation rate was increased by 130%. Furthermore, when both glutamine and alanine were added together to the infusion media, the alcohol oxidation rate increased by as much as 190%, and the rate of urea nitrogen production increased by up to 200%. The addition of glutamine (5.0mM) alone to the infusion media did not accelerate the alcohol oxidation rate. The increases in the rates of alcohol oxidation and urea nitrogen production through the addition of alanine and glutamine indicate that these amino acids have contributed to the enhanced supply of pyruvate through the urea cycle. Based on these results, it is concluded that the dietary supplementation of alanine and glutamine could contribute to increased alcohol detoxification through the urea cycle, by enhancing the supply of pyruvate and $NAD^+$to ensure accelerated rates of alcohol oxidation.

• Bulletin of the Korean Chemical Society
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• 제16권5호
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• pp.410-416
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• 1995

The proton transfer energies of gas phase glycine and alanine and those of hydrated glycine and alanine were calculated both with Hartree-Fock and $M{\Phi}ller-Plesset$ ab initio molecular orbital (MO) calculations with 6-31G** basis set. The transition states of the proton transfer of gas phase glycine was also investigated. For zwitterions, both for glycine and alanine, the water bound to -NH3+ site stabilize the complex more compared with the water bound to -CO2-. The proton transfer energy, ΔEpt, of glycine, alanine, mono-hydrated glycine, mono-hydrated alanine, di-hydrated glycine and di-hydrated alanine were obtained as 30.78 (MP2: 22.57), 31.43, 23.99 (MP2: 17.00), 24.98, 22.87, and 25.63 kcal/mol, respectively. The activation energy for proton transfer from neutral (Nt) glycine to zwitterion (Zw) glycine, Ea, was obtained as 16.13 kcal/mol and that for reverse process, Ear, was obtained as 0.85 kcal/mol. Since the transition state of the proton transfer of gas phase glycine locate near the glycine zwitterion on the potential energy surface and the shape of the potential well of the zwitterion is shallow, the zwitterion easily changed to neutral glycine through the proton transfer.

• Bulletin of the Korean Chemical Society
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• 제21권12호
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• pp.1217-1221
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• 2000

L-alanine dehydrogenase from Bacillus subtilis exhibits allosteric kinetic properties in the presence of $ZN^{2+}$. $ZN^{2+}$ induces the binding of substrate (L-alanine) to be cooperative at pH 8.0. The effect of pH variation between pH 7.0 and pH 10.0 on the inhibition by $ZN^{2+}$ correlates with the pH effect on the $K_m$ values for L-alanine within these pH range indicating that $ZN^{2+}$ and substrate compete for the same site. No such cooperativity is induced by $ZN^{2+}$ when the reaction is carried out at pH 10. At this higher pH, $ZN^{2+}$ binds with the enzyme with lower affinity and noncompetitive with respect to L-alanine. Inhibition of L-alanine dehydrogenase by $ZN^{2+}$ depends on the ionic strength. Increase in KCI concentration reduced the inhibition, but allosteric property in $ZN^{2+}$ binding is conserved. A model for the regulatory mechanism of L-alanine dehydrogenase as a noncooperative substrate-cooperative cofactor allosteric enzyme, which is compatible in both concerted and the sequential allosteric mechanism, is proposed.

• 약학회지
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• 제8권2호
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• pp.45-47
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• 1964

Two new orotic acid derivatives orotyl-DL-alanine and orotyl-L-tyrosine were synthesized. They were obtained as high melting crystalline masses by condensing DL-alanine and L-tyrosine each with orotyl chloride in aqueous sodium hydroxide solution, followed by acidifying the reaction mixture.

• 분석과학
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• 제30권6호
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• pp.303-311
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• 2017

잠재지문 증강시약인 1,2-indandione (1,2-IND) 용액을 사용하여 종이에 유류된 족적의 형광을 얻는 방법을 연구하였다. 인쇄물이 출력된 A4 용지에 유류된 dry origin 및 wet origin 족적에 아미노산의 일종인 DL-alanine 용액과 아미노산 검출시약인 1,2-IND 용액을 뿌려서 DL-alanine-1,2-IND 이성분착물을 만들었다. 이 이성분착물은 족적에 있는 미량의 금속성분과 반응하여 광발광을 내는 삼성분착물을 형성함으로써 족적의 형광을 관찰할 수 있었다. 그러나 1,2-IND 용액 대신 5-methylthioninhydrin (5-MTN) 용액을 이용하면 처리 조건을 동일하게 유지해도 족적의 형광이 일정하게 관찰되지 않았다. DL-alanine 용액과 1,2-IND 용액으로 처리한 족적을 다양한 온도조건 (30, 40, $50^{\circ}C$)과 다양한 습도조건 (30, 40, 50, 60 % RH)에서 보관한 결과 온도와 습도가 높을수록 족적과 바탕면의 대조비가 감소하였다. DL-alanine 용액과 1,2-IND 용액으로 처리한 족적을 $30^{\circ}C$, 30 % RH에서 1 h 동안 보관하면 족적의 최적 형광을 얻을 수 있었다. 저자들이 개발한 방법의 감도를 black gelatin lifting, 2,2'-dipyridil 용액 처리 방법, 8-hydroxyquinoline 용액 처리방법의 감도와 비교하였다. 그 결과 저자가 개발한 방법의 감도는 gelatin lifting 방법보다는 떨어졌으나 2,2'-dipyridil 용액 혹은 8-hydroxyquinoline 용액 처리방법보다는 우수하였다.

• Journal of Applied Biological Chemistry
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• 제54권4호
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• pp.231-237
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• 2011

A gene encoding a putative alanine racemase in Xanthomonas. oryzae pv. oryzae was cloned, expressed and characterized. Expression of the cloned gene was performed in Escherichia coli BL21(DE3)pLys using a pET-21(a) vector harbouring $6{\times}histidine$ tag. Purification of the recombinant alanine racemase by affinity chromatography resulted in major one band by sodium dodecyl sulfate polyacryl amide gel electrophoresis analysis, showing about 45 kDa of molecular weight. The alanine racemase gene, cloned in this experiment, appears to be constitutively expressed in X. oryzae, as analyzed by reverse transcriptase polymerase chain reaction. The enzyme was the most active toward L-alanine and secondly D-alanine, showing a racemic reaction, thus the enzyme is considered as an alanine racemase. The enzyme was considerably activated by addition of pyridoxal-5-phosphate (PLP), showing that 75% increase in activity was observed at 0.3 mM, compared with control. D-Cysteine as well as L-cysteine significantly inhibited the enzyme activity. The inhibitions by cysteines were more prominent in the absence of PLP, showing 9 and 5% of control activity at 2 mM of addition, respectively. The enzyme was the most active at pH 8.0 and more stable at alkaline pHs than acidic pH condition.

• 응용화학
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• 제15권1호
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• pp.37-40
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• 2011

A chemiluminescent method with silver nanoparticles for determination of L-alanine has been presented. The chemilumiscence intensity was further enhanced by silver nanoparticles in the luminol system by its catalytic role. The silver nanoparticles enhanced chemiluminescent method is applicable for the determination of an amino acid such as alanine. When alanine was introduced to the luminol system with silver nanoparticles, chemiluminescence intensity was reduced with the concentration of the added alanine. The effects of pH, concentrations of luminol, hydrogen peroxide and silver nanoparticles on the chemiluminescence intensity were investigated. The calibration curve for L-alanine was linear over the range from 6.60×10^-8 M to 4.00×10^-7 M, coefficient of correlation was 0.996 and detection limit was 3.5×10^-9 M under the optimal conditions of 4.0×10^-3 M, 4.0×10^-2 M, 4.0×10^-4 M, 12.8 for the concentration of luminol, H₂O₂, silver nanoparticles and pH, respectively.