• Journal of Veterinary Clinics
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• v.15 no.1
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• pp.14-21
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• 1998

Ultrasonogram for kidney, spleens liver, intestine and heart was evaluated 11 Chriu horses and 14 Thoroughbred horse. The kidney was determined at both flan and both 17th intercostal spaces. The spleen was determined at the left 13-17 intercom spacer and the liver was determined at the right 7-13 intercostal space. The heart was determined at the right 4-6 intercostal space and left 3-6 intercostal space. The length, of rig kidney at the Thoroughbred horse, Thoroughbred foul, Cheju horse and Cheju foul were 16.2, 12.6, 13.1 and 11.2 mm, respectively. The width of right kidney at the Thoroughbed horse, Thorughbred foul, Cheju horse and Cheju foul were 5.4, 4.3, 4.6 and 4.2 mm, respectively. The depth of right kidney at the Thoroughbred horsed Thoroughbred foul, Cheju horse and Chrju foul were 5.2, 4.4, 4.5 and 4.3 mm, respectively. Similar ultrasonographic measurements were obtained for the left kidney, The left ventricular end-diastolic diameter at the Thoroughbred horse, Thoroughbred fouls Cheju horst and Cheju foul were 107, 83, 85 and 73 mm, respectively. The left ventricular end-systolic diameter were at the Thoroughbred horse, Thoroughbred foul, Cheiu horse and Cheiu foul were 63, 52, 53 and 45 mm, respectively. Also, the interventricular septum in end-diastole, interventricular septum in end-systoles left ventricular wall end-diastoles left ventricular wall end-systoles right ventricular end-diastole diameter, aorta and left atrium at t Thoroughbred horse, Thoroughbred foul, Chriu horse and Chriu foul were measured. Experimental renal stone and enterolith of colon were observed by ultrasonography.

• Animal Bioscience
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• v.34 no.2
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• pp.312-319
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• 2021

Objective: Stress-induced cytotoxicity caused by xenobiotics and endogenous metabolites induces the production of reactive oxygen species and often results in damage to cellular components such as DNA, proteins, and lipids. The cytochrome P450 (CYP) family of enzymes are most abundant in hepatocytes, where they play key roles in regulating cellular stress responses. We aimed to determine the effects of the antioxidant compound, methylsulfonylmethane (MSM), on oxidative stress response, and study the cytochrome P450 family 3 subfamily A (CYP3A) gene expression in fetal horse hepatocytes. Methods: The expression of hepatocyte markers and CYP3A family genes (CYP3A89, CYP3A93, CYP3A94, CYP3A95, CYP3A96, and CYP3A97) were assessed in different organ tissues of the horse and fetal horse liver-derived cells (FHLCs) using quantitative reverse transcription polymerase chain reaction. To elucidate the antioxidant effects of MSM on FHLCs, cell viability, levels of oxidative markers, and gene expression of CYP3A were investigated in H2O2-induced oxidative stress in the presence and absence of MSM. Results: FHLCs exhibited features of liver cells and simultaneously maintained the typical genetic characteristics of normal liver tissue; however, the expression profiles of some liver markers and CYP3A genes, except that of CYP3A93, were different. The expression of CYP3A93 specifically increased after the addition of H2O2 to the culture medium. MSM treatment reduced oxidative stress as well as the expression of CYP3A93 and heme oxygenase 1, an oxidative marker in FHLCs. Conclusion: MSM could reduce oxidative stress and hepatotoxicity in FHLCs by altering CYP3A93 expression and related signaling pathways.

• Archives of Pharmacal Research
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• v.15 no.3
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• pp.229-233
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• 1992

The pKa value of histidine-51 residue was determined by the pH dependency of contents of NADH bound to the active site in the orse liver alcohol dehydrogenase and % inactivation with diethyl pyrocarbonate treatment of the enzyme. The pKa for His-51 was -7.15 in the ternary complex and -6.7 in the enzyme itself.

• Archives of Pharmacal Research
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• v.20 no.2
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• pp.115-121
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• 1997

Ile-269 in horse liver alcohol dehydrogenase isoenzyme S(HLADH-S) was mutated to serine by phosphorothioate-based site-directed mutagenesis in order to study the role of the residue in coenzyme binding. The specific activity of the mutant(1269S) enzyme to ethanol was increased 49-fold. All turnover numbers of 1269S enzyme toward 9 primary alcohols were increased. The mutant enzyme showed 3.6, 4.6, 11.6-fold higher catalytic efficiency for $5{\beta}$-androstane-3, 17-dione, $5{\beta}$-cholanic acid-3-one and retinal than wild-type, respectively. The reaction mechanism of 1269S enzyme was ordered bi bi as wild-type's. These results indicate that the hydrophobic interaction of Ile-269 residue with coenzyme plays an important role in dissociation of coenzyme from enzyme-coenzyme complex, which has been known as the rate limiting step of ADH reaction.

• Archives of Pharmacal Research
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• v.22 no.1
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• pp.13-17
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• 1999

The kinetic constants and the reaction mechanism of the K228G mutant horse liver alcohol dehyrogenase isoenzyme E (HLADH-E) were compared to the wild-type enzyme. All the Km and Ki constants of the mutant enzyme for NAD+, ethanol, acetaldehyde and NADH were larger than those of the wild-type enzyme. The dissociation constants for the NADH and $NAD^{+}$ (Kiq and Kia) were greatly increased by 130-and 460-fold, respectively. The product inhibition patterns suggested that the reaction mechanism of the mutant enzyme was changed to Random Bi Bi. These results could attribute to the increase in the dissociation rate of coenzyme with the substitution at Lys-228 residue.

• Archives of Pharmacal Research
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• v.18 no.2
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• pp.100-104
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• 1995

Lys-228 in horse liver alcohol dehydrogenase isoenzyme E(HLADH-E) was mutated to glycineby site-directed mutagenesis. The specific activity of the mutant enzyme was increased about 4-fold nad Michaelis constants for $NAD^+(K_a){\;}and{\;}NADH(K_q)$ increased by about 350-and 50-fold, respectively. The wild-type enzyme and K228TG mutant enzyme were treated with ethylacetimidate. Acetimidylation of the wild-type enzyme increased the activity about 10-fold, but the mutant enzyme ws little affected. These results confirm that Lys-228 residue plays an important role in the activity of the enzyme through forming the hydrogen bond with adenosine ribose of $NAD^+$.

• Korean Journal of Veterinary Service
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• v.34 no.2
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• pp.187-190
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• 2011

The Thoroughbred horse was an approximately 4-years-old castrated male with highly emaciation, nasal epistaxis and subsequently died. Gross necropsy revealed epistaxis and hyperemia on the lung, multiple hemorrhage in muscle, and liver was focally attached to the peritoneum with fibrin. According to polymerase chain reaction (PCR), Equine herpes virus type 1 and 4 (EHV type 1, 4) was detected in the lung and trachea. In bacterial culture from kidney, liver, spleen, muscle and blood, Streptococcus equi subsp. zooepidemicus was isolated. Based on the gross lesion and PCR, this horse was diagnosed as EHV type 1, 4 and S. zooepidemicus coinfection.

• Journal of Physiology & Pathology in Korean Medicine
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• v.18 no.6
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• pp.1723-1727
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• 2004

We investigated the activity and stability of alcohol dehydrogenase from horse liver (HLADH) under the electric stimulation. The activity and stability of alcohol dehydrogenase depended on electric output voltaqe, stimulation time, pulse duration and pulse interval, and temperature. HLADH retained about 23% of its activity in buffer but 78% in 10% trehalose solution under electric stimulation with 10V, 10min, The stabilizing of enzymes against electric stimulation by stabilizing additives showed a great potential use of enzymes in biotechnology and medical engineering fields.

• Journal of the Korean Chemical Society
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• v.45 no.1
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• pp.61-66
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• 2001

Stabilized Cross-linking Enzyme Crystals(CLEC) can be used as not only biocatalysts but also as enzyme sensors. PMS(Phenylmethyl Sulfate)was shown more efficience than any other electron mediator transfers toward HLADH(Horse Liver Alcohol Dehydrogenase)that were examined. NQS(naphtoquinonesulphonate), phenothiazine and ferrocene aldehyde had respectively just 52%, 37%, 35% electron transfer efficiency as compared to PMS . HLADH-CLEC was very stable toward elctron transfer mediators such as PMS, NQS and ferrocene aldehyde in which HLADH-solution was unstable.

• Bulletin of the Korean Chemical Society
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• v.9 no.1
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• pp.44-48
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• 1988

The feasibility of the reduction of nortricyclanone (1) as a chemical probe for testing the proposed radical mechanism for NAD-dependent horse liver alcohol dehydrogenase (HLADH) reactions has been examined using computer graphics modeling. The resutls of this study suggest that the radical ring-opening of this probe molecule may involve too substantial a geometry reorganization for the molecule to serve as a chemical probe in detecting the possible presence of the radical intermediates in the HLADH reactions. This result suggests that one should exercise caution in extrapolating results obtained from chemically based radical probes in the solution phase to the topologically constrained systems such as enzyme-substrate reactions.