• Journal of the Korean Magnetic Resonance Society
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• v.10 no.1
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• pp.115-125
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• 2006

Hippuryl-L-histidyl-L-leucine(HHL) is widely used as a substrate of angiotensin converting enzyme(ACE) cleaving the neurotransmitter angiotensin(I) to the octapeptide angiotensin(II). The structure of the substrate molecules should provide information regarding the geometric requirements of the ACE active site. For the purpose of determination of in vivo reaction, metallo(Cu, Zn)-HHL complexes were synthesized and the degree of complex formation were identified by MALDITOF, ESI mass spectrometric analysis. Tn addition, the pH-dependent species distribution curves were obtained by potentiometric titration. Nitrogen atoms of imidazole ring and oxygen atom of caboxylate groups in the peptide chain were observed to be participated in the metal complex formation. After purification of complexes further structural characterization were made by utilizing UV-Vis, electrochemical methods and NMR. Complete NMR signal assignments were carried out by using 2D-spectrum techniques COSY, TOCSY, NOESY, HETCOR. A complex that two imidazole and carboxylate groups are asymmetrically participating to coordination mode was predicted to the solution-state structure of $Cu(II)-HHL_2$ based on $^{13}C-NMR$ signal assignment and NOE information.

• Food Science of Animal Resources
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• v.29 no.6
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• pp.719-725
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• 2009

Heterocyclic aromatic amines (HCAs) are potent mutagens and possible human carcinogens that are formed during the heating of protein-rich foods. The effects of preheating treatment of beef patties using a microwave prior to frying at $220^{\circ}C$ for 10 min on each side on the reduction of HCAs (amino-carbolines and amino-imidazo-azaarenes) were evaluated. The amount of HCAs was then evaluated by solid-phase extraction and high pressure liquid chromatography (HPLC) analysis. The beef patties were treated by microwaving for various times (0, 1, 1.5, 2, or 3 min) before pan-frying. The results revealed the presence of 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2), 3-amino-1,4-dimethyl-5H-pyrido-[4,3-b] indole (Trp-P-1), 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole (Glu-P-1), 2-aminodipyrido[1,2-a:3',2'-d]imidazole (Glu-P-2), 9H-pyrido[3,4-b]indole (Norharman), 1-methyl-9H-pyrido[3,4-b]indole (Harman), 2-amino-9H-pyrido[2,3-b] indole ($A{\alpha}C$), 2-amino-3,8 dimethylimidazo[4,5-f]-quinoxaline (MeIQx) and 2-amino-1-methyl-6-phenylimidazo[4,5-b]-pyridine (PhIP) in all samples. However, microwave pretreatment for 1 min inhibited the formation of these HCAs by up to 90% when compared to the control.

• Bulletin of the Korean Chemical Society
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• v.35 no.8
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• pp.2419-2422
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• 2014

The syntheses and crystal structures of a three-dimensional (3D) coordination network $[Zn_4(2-mBIM)_5-(C_2H_6NCOO)(HCOO)({\mu}-OH)]{\cdot}DMF$ ($1{\cdot}$DMF; 2-mBIM = 2-methylbenzimidazolate) and a two-dimensional (2D) layer $[Zn_2(2-mBIM)_3(HCOO)(H_2O)]{\cdot}DMF$ ($2{\cdot}DMF$) are reported. Different structures were produced depending on the ratio of reactants. Structurally, 1 illustrates the formation of a unique framework based on a 2-mBIM bridge with the side group on an imidazole ring, while 2 possesses a honeycomb layer built up purely from imidazolates. For gas sorption, $CO_2$ is adsorbed on the activated phase of 1 but $N_2$ is not taken up.

• Korean Journal of Food Science and Technology
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• v.32 no.5
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• pp.1158-1167
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• 2000

To produce ${\beta}-cyclodextrin({\beta}-CD)$, a cyclodextrin glucanotransferase(CGTase) producing Aspergillus sp. CC-2-1 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of CGTase reached to the maximum when the wheat bran medium containing 0.1% albumin, 2% $(NH_4)_2S_2O_8$, 2% soluble starch and 0.2% $KH_2PO_4$ was cultured for 5 days at $37^{\circ}C$. The purity of CGTase was increased by 13.14 folds after DEAE-cellulose ion exchange chromatography and Sephadex G-100, G-150 gel filtration and the specific activity was 172.14 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of CGTase was estimated to be 27,800 by Sephadex G-100 gel filtration and SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the CGTase activity were 9.0 and $80^{\circ}C$, respectively. The enzyme was stable in pH $8.0{\sim}11.0$ at $60{\sim}80^{\circ}C$. The activity of purified enzyme was activated by $K^+,\;Cu^{2+}$ and $Zn^{2+}$. The activity of the CGTase was inhibited by the treatment with 2,4-dinitrophenol and iodine. The result suggests that the purified enzyme has phenolic hydroxyl group of tyrosine, histidine imidazole group and terminal amino group at active site. The reaction of this enzyme followed typical Michaelis-Menten kinetics with the $K_m$ value of 18.182 g/L with the $V_{max}$ of 188.68 ${\mu}mole/min$. The activation energy for the CGTase was calculated by Arrhenius equation was 1.548 kcal/mol.

• Bulletin of the Korean Chemical Society
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• v.16 no.10
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• pp.912-915
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• 1995

Ornidazole, C7H10ClN3O3, crystallizes in the triclinic, space group P1^, with a=13.605(2), b=14.054(1), c=8.913(5) Å, α=71.59(2), β=78.73(2), γ=64.86(1)°, μ=3.26 cm-1, Dc=1.499 g/cm3, Dm=1.497g/cm3, F(000)=684, and z=6. Intensities for 2693 unique reflections were measured on a CAD4 diffractometer with graphite-monochromated Mo-Kα radiation. The structure was solved by direct method and refined by block-diagonal least squares to a final R of 0.081 (Rw=0.047) for 1952 reflections with Fo>3σ (Fo). The asymmetric unit contains three independent molecules of the title compound. The bond lengths and bond angles are comparable with the values found in the other nitro-substituted compounds. The nitro groups are rotated (6.9°, 6.6°, 2.6° for the three independent molecule, respectively) about the C-N axes from the imidazole planes. The crystal structures are linked by two intermolecular hydrogen bonds of O-H---N type and one intermolecular hydrogen bond of O-H---O type.

• Journal of the Korean Magnetic Resonance Society
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• v.10 no.2
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• pp.163-174
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• 2006

Luteinizing Hormone Releasing Hormone(LHRH) is a decapeptide neurotransmitter known to be regulated by metal ions in the hyperthalamus. Zn-binding LHRH complex was systhesized, and zinc-LHRH complex was studied to understand what kinds of structural modifications would be critical in the LHRH releasing mechanism. Both nonexchangeable and exchangeable $^1H-NMR$ signal assignments were accomplished by pH-dependent and COSY NMR experiments. In addition, $^1H-NMR$ chemical shift changes of a-proton and peptide NH NMR signals at different pH condition, and $^1H-NMR$ signal differences between metal free and metallo-LHRH complex was monitored. NMR signals exhibit that primary metal-binding sites are nitrogens donor of imidazole ring and Arg, and peptide oxygen of Pro-His in the sequence. Structure obtained in this study has a cyclic conformation which is similar to that of energy minimized, and exhibits a specific a-helical turn with residue numbers $(2{\sim}7)$ out of 10 amino acids.

• Journal of the Korean Chemical Society
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• v.33 no.1
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• pp.3-10
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• 1989

In order to obtain a clue in understanding enzymatic hydrolysis in which the His-Cys moieties of papain protease is involved, we prepared cationic peptide-sufactants bearing histidyl, cysteinyl, and both histydyl and cysteinyl residues. Their catalytic efficiency toward the hydrolysis of PNPL were investigated in comicellar phases formed with $N^{+}C_{2}CysC_{12}$, $N^{+}C_{2}HisC_{12}$, $N^{+}C_{2}HisCysC_{12}$ increased markedly in the same order compared with that of $N^{+}C_{2}AlaC_{12}$. The markedly increased catalytic effects are attributed to the imidazole groups of $N^{+}C_{2}HisC_{12}$ and the thiol groups of $N^{+}C_{2}CysC_{12}$, and the large catalytic efficiency of $N^{+}C_{2}HisCysC_{12}$, is considered due to the interaction of the imidazole and the thiol groups. In order to investigate catalytic activities, rate constants for the functional groups, km* and dissociation constants, pKa have been determined. The results showed that $k^{\ast}_m$ and pKa of the imidazole groups were $7.91{\times}10^{-4}S^{-1}$ and 6.49, and those of the thiol groups were $6.00{\times}10^{-4}S^{-1}$ and 10.50. The catalytic effects of comicellar systems on the hydrolysis of p-nitrophenyl esters has increased according to the increasing size of the alkyl carbon number. Therefore, the catalytic effects have been increasing by the interaction of micellar hydrophobic parts and substrates as well as action of the functional groups.

• Journal of the Korean Chemical Society
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• v.23 no.4
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• pp.248-258
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• 1979

Glucose 6-phosphate dehydrogenase of Leuconostoc mesenteroides which was purifid by an affinity chromatography was studied on the characterization, kinetics and chemical modification. The apparent molecular weight of the enzyme was 112,000 by the gel filtration method of Sephadex G-200 column. The optimum temperature of $NAD^+$-linked reation was 50$^{circ}C$ and the activation energy and the heat of inactivation were 8.36 kcal/mole and -58.2kcal/mole, respectively. The steady state kinetic study showed KG6P, Kemp, and CX KNADP to be 76.9 PM, 7.46${\mu}M$ and 7.14 ${\mu}M$, respectively, and KGGP, KNAD,and aKNm to be 53.7${\mu}M$, 115.2${\mu}M$ and 702.2${\mu}M$ for the $NAD^+$-linked reaction at pH 7.8, optimum pH. The pH dependent kinetic constants suggested that the two ionizing groups whose pKa is 7.2 .and pKb is 9.0-9.6 were involved in the enzyme-substrate interaction. Evidence by photooxidation and carboxymethylation of the enzyme suggested that the imidazole group of histidine with pKa group may participate in the catalytic site.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.21 no.2
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• pp.432-439
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• 2020

This study examined the metabolites in different roughage to concentrate ratios using proton nuclear magnetic resonance spectroscopy (1H-NMR). Six lactating cows were divided into two groups that were fed different roughage to concentrate ratios (HR group = 8:2, HC group = 2:8). Feces samples were collected individually at one time, and the metabolites were analyzed using an SPE-800 MHz NMR-MS system. The metabolites were identified and quantified using a Chenomx NMR suite 8.4. Metabolic pathway analysis and principal component analysis were conducted using a Metaboanalyst 4.0. Statistical analysis was performed using a Dunnett's test on the SAS program. As a result, several metabolites were identified, and among them, 77 metabolites were used in statistical analysis. The levels of twelve metabolites were significantly higher in the HC group: succinate, dimethylamine, histamine, homovanillate, thymol, acetate, propionate, butyrate, isovalerate, valerate, imidazole, N-nitrosodimethylamine, and O-acetylcholine. In the HC group, the concentrations of all metabolites were higher than in the HR group, and the metabolic pathway was also different. This study is expected to be useful for a variety of livestock studies by 1H-NMR because it examined the change in metabolites in the body metabolism and microorganisms.

• Bulletin of the Korean Chemical Society
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• v.30 no.9
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• pp.1963-1966
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• 2009

L-Proline has been found to be an efficient organocatalyst for one-pot synthesis of 2,4,5-triaryl substituted imidazole by the reaction of an aldehyde, a benzil and an ammonium acetate. The short reaction time and excellent yields making this protocol practical and economically attractive.