• Bulletin of the Korean Chemical Society
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• v.33 no.5
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• pp.1561-1565
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• 2012

The structures of the four lowest alanine conformers, along with their radical cations and the effect of ionization on the intramolecular proton transfer process, are studied using the density functional theory and MP2 method. The energy order of the radical cations of alanine differs from that of the corresponding neutral conformers due to changes in the basicity of the $NH_2$ group upon ionization. Ionization favors the intramolecular proton transfer process, leading to a proton-transferred radical-cation structure, [$NH_3{^+}-CHCH_3-COO{\bullet}$], which contrasts with the fact that a proton-transferred zwitterionic conformer is not stable for a neutral alanine in the gas phase. The energy barrier during the proton transfer process is calculated to be about 6 kcal/mol.

• Asian-Australasian Journal of Animal Sciences
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• v.4 no.4
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• pp.369-375
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• 1991

A series of in vitro incubation studies with washed rumen bacteria were conducted to determine the influence of incubation time and concentrations of peptides, alanine, ammonia nitrogen and carbohydrate on the rate of peptide disappearance and on bacterial growth. Disappearance rate of tri-alanine (ala3) under various conditions was between 30.6 and $58.2mg\;hr^-$ per gram bacterial dry matter. Ala3 was removed from the incubation medium in an almost linear fashion as incubation time and ala3 concentration was increased. Washed rumen bacteria utilized ala3 faster than di-l-alanine (ala2) at all concentrations. Adding 9mM carbohydrate significantly increased ala3 disappearance, but level of ammonia nitrogen had no influence on ala3 disappearance. The presence of alanine in the medium significantly lowered ala3 utilization by rumen bacteria. Bacterial dry matter and nitrogen growth yield were not influenced by alanine and peptides when incubation medium already contained a sufficient level of ammonia nitrogen. Increased ammonia nitrogen in the presence of ala3 did not stimulate bacterial growth. Carbohydrate significantly increased bacterial dry matter and nitrogen growth as expected. Results indicate that the rate of peptide utilization by rumen bacteria may be altered by type and concentration of peptides, and energy supply, and this may be mediated through changes in numbers and type of bacteria.

• Korean Journal of Materials Research
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• v.15 no.6
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• pp.426-430
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• 2005

Chemical mechanical polishing (CMP) is an essential process in the production of integrated circuits containing copper interconnects. The effect of alanine in reactive slurries representative of those that might be used in copper CMP was studied with the aim of improving selectivity between copper(Cu) film and tantalum-nitride(TaN) film. We investigated the pH effect of nano-colloidal silica slurry containing alanine through the chemical mechanical polishing test for the 8(inch) blanket wafers as deposited Cu and TaN film, respectively. The copper and tantalum-nitride removal rate decreased with the increase of pH and reaches the neutral at pH 7, then, with the further increase of pH to alkaline, the removal rate rise to increase soddenly. It was found that alkaline slurry has a higher removal rate than acidic and neutral slurries for copper film, but the removal rate of tantalum-nitride does not change much. These tests indicated that alanine may improve the CMP process by controlling the selectivity between Cu and TaN film.

• Progress in Medical Physics
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• v.1 no.1
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• pp.31-42
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• 1990

The finding of long lived free radicals produced by ionizing radiation in organic crystals and the quantification of this effect by electron spin resonance(ESR) spactroscopy has proven excellent dosimetric applicability. The tissue equivalent alanine dosimeter also appear appropriate for radiation therapy level dosimetry. The dose measurement was performed in a Rando phantom using high energy photons as produced by high energy medical linear accelerator and cobalt-60 teletherapy unit. The absorbed dose range of the ESR/alanine dosimetry system could be extended down to 0.1 Gy. The response of the alanine dosimeters was determined for photons at different therapeutic dose levels from less than 0.1 Gy to 100 Gy and the depth dose measurements were carried out for photon energies of 1.25MeV, 6 and 10 MV with alanine dosimeters in Rando phantom. Comparisons between ESR/alanine in a Rando phantom and ion chamber in a water phantom were made performing depth dose measurements to examine the agreement of both methods under field conditions.

• Microbiology and Biotechnology Letters
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• v.33 no.4
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• pp.319-321
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• 2005

We have previously reported the isolation and characterization of peptides binding to $TiO_{2}$ nanoparticles from phage display peptide libraries. One of the peptides (PEP9) was selected and mutant peptide-displaying phages were produced by alanine scanning mutagenesis. The mutant phages were subjected to binding analysis to $TiO_{2}$ nanoparticles. When the proline at residue 4 was substituted by alanine, the binding activity was reduced to $10\%$ of that of wild type PEP9. Substitution of valine at residue 2, serine at residue 3, and isoleucine at residue 5 also decreased the binding to $40\%$. Based on these observations, we concluded that the three dimensional structure generated by residues 2-5 was the critical factor for the binding between PEP9 and the nanoparticle.

• BMB Reports
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• v.42 no.1
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• pp.47-52
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• 2009

Alanine racemase catalyzes the interconversion of L-alanine and D-alanine and plays a crucial role in spore germination and cell wall biosynthesis. In this study, alanine racemase produced by Bacillus anthracis was expressed and purified as a monomer in Escherichia coli and the importance of lysine 41 in the cofactor binding octapeptide and tyrosine 270 in catalysis was evaluated. The native enzyme exhibited an apparent $K_m$ of 3 mM for L-alanine, and a $V_{max}$ of $295\;{\mu}moles/min/mg$, with the optimum activity occurring at $37^{\circ}C$ and a pH of 8-9. The activity observed in the absence of exogenous pyridoxal 5'-phosphate suggested that the cofactor is bound to the enzyme. Additionally, the UV-visible absorption spectra indicated that the activity was pH independece, of VV-visible absorption spectra suggests that the bound PLP exists as a protonated Schiff's base. Furthermore, the loss of activity observed in the apoenzyme suggested that bound PLP is required for catalysis. Finally, the enzyme followed non-competitive and mixed inhibition kinetics for hydroxylamine and propionate with a $K_i$of $160\;{\mu}M$ and 30 mM, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.4
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• pp.336-341
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• 1983

A study on the oxidation effect of some amino acids(glutamic acid, phenylalanine, alanine) addition to the linoleic acid emulsion was conducted. Amino acid solutions in concentrations of $10^{-2}$, $10^{-3}$ and $10^{-4}M$ were mixed with equal volume of linoleic acid emulsions. The prepared samples were incubated at $60{\pm}1^{\circ}C$ and the extent of diene conjugation and TBA values were measured by using the UV visible spectrophotometer. The results were as follows: 1) From the extent of diene conjugation, we found that the addition of phenylalanine and alanine prolonged the induction period and the addition of glutamic acid shortened. There was an optimum concentration for each amino acid to act as an antioxidant during the induction period. The optimum concentration of alanine was $10^{-3}M$ and that of phenylalanine was $10^{-2}M$. 2) The results of TBA values showed that three amino acids possesed antioxidant activity after the induction period. There was also an optimum concentration to act as antioxidant after the induction period. The optimum concentrations of glutamic acid, phenylalanine, and alanine were $10^{-2}$, $10^{-3}$, and $10^{-3}M$, respectively.

• Korean Journal of Clinical Laboratory Science
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• v.53 no.3
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• pp.241-248
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• 2021

The present study was conducted to assess the relationship between aspartate aminotransferase/alanine aminotransferase (AST/ALT) ratio and pulse pressure in Korean adults with hypertension. Data from 1,515 adults from the sixth Korean National Health and Nutrition Examination Survey (KNHANES VI-3, 2015) were analyzed. There were several key findings in the present study. First, aspartate aminotransferase (odds ratio [OR], 1.018; 95% confidence interval [CI], 1.002 to 1.033), alanine aminotransferase (OR, 0.982; 95% CI, 0.969 to 0.996), and aspartate aminotransferase/alanine aminotransferase ratio (OR, 1.367; 95% CI, 1.027 to 1.819) were the independent factors determining high pulse pressure. Second, after adjusting for related variables [age, gender, smoking, alcohol consumption, regular exercise, total cholesterol (TC), triglycerides (TGs), high-density lipoprotein-cholesterol (HDL-C), fasting plasma glucose (FPG), body mass index (BMI), and waist circumference (WC)], the ORs of high pulse pressure with the 1st quartile as a reference were significantly higher in the 4th quartile of aspartate aminotransferase/alanine aminotransferase ratio [1.632 (95% CI, 1.113~2.393)]. The high pulse pressure was positively associated with aspartate aminotransferase and alanine aminotransferase/alanine aminotransferase ratio in Korean adults with hypertension, but was inversely associated with alanine aminotransferase.

• Journal of Microbiology
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• v.40 no.1
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• pp.33-37
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• 2002

An enzymatic reaction for the production of D-alanine from D-aspartic acid and pyruvate as substrates by a thermostable D-amino acid aminotransferase (D-AAT) was investigated at various conditions In the temperature range of 40-70$\^{C}$ and pH range of 6.0-9.5. The D-AAT was produced with recombinant E. coli BL21, which hosted the chimeric plasmid pTLK2 harboring the D-AAT from the novel thermophilic Bacillus sp. LK-2. The enzyme reaction was shown to follow the Ping Pong Bi Bi mechanism. The K$\_$m/ values for D-aspartic acid and pyruvate were 4.38 mar and 0.72 mM, respectively. It was observed that competitive inhibition by D-alanine, the product of this reaction, was evident with the inhibition constant K$\_$i/ value of 0.1 mM. A unique feature of this reaction scheme is that the decorboxylation of oxaloacetic acid, one of the products, spontaneously produces pyruvate. Therefore, only a catalytic amount of pyruvate is necessary for the enzyme conversion reaction to proceed. A typical time-course kinetic study skewed that D-alanine up to 88 mM could be produced from 100 mM of D-aspartic acid with a molar yield of 1.0.

• Journal of Microbiology and Biotechnology
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• v.13 no.4
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• pp.628-631
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• 2003

The recombinant alanine dehydrogenase (ADH) from E. coli containing Thermus caldophilus ADH was purified to homogeneity from a cell-free extract. The enzyme was purified 38-fold with a yield of 68% from the starting cell-free extract. The purified enzyme gave a single band in polyacrylamide gel electrophoresis, and its molecular weight was estimated to be 45 kDa. The pH optimum was 8.0 for reductive amination of pyruvate and 12.0 for oxidative deamination of L-alanine. The enzyme was stable up to $70^{\circ}C$. The activity of the enzyme was inhibited by 1 mM $Zn^{2+}$, 20% hexane, and 20% $CHCl_3$. However, 10 mM $Mg^{2+}$ and 40% propanol had no effect on the enzyme activity. The Michaelis constants ($K_m$) for the substrates were $50\;\mu\textrm{M}$ for NADH, 0.2 mM for pyruvate, 39.4 mM for $NH_4+$, 2.6 mM for L-alanine, and 1.8 mM for $NAD^+$.