• Korean Journal of Fisheries and Aquatic Sciences
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• v.43 no.1
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• pp.12-17
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• 2010

Wild and cultured fish including olive flounder, sea bass, rock bream, yellowtail, gray mullet, gizzard shad, black rockfish, red seabream and squid were collected from a fish market located on the coast of Korea, and the antibiotic content of their muscle was investigated. Tetracycline group antibiotics were not detected in the 108 individuals of 9 species of wild fish. However, oxytetracycline (OTC) and tetracycline(TC) were detected in some samples of the 111 individuals in 7 cultured live fish species. The detected ranges of OTC and TC were ND~ 0.06 and ND~ 0.03, respectively. Five different fluoroquinolone antibiotics were also tested for, but were not detected in the wild fish species. Only small amount of criprofloxacin(ND~0.029 mg/kg) were detected in a few cultured fish samples. Oxolinic acid was not detected in either wild and cultured fish samples. Results showed that even very low levels of antibiotics could be detected by the testing methods used. Antibiotics were identified in a few fish samples but levels were far below the maximum allowable limits of the Korean Food Code, and the safety of fish being sold in markets, with regard to antibiotic levels, was confirmed.

• Journal of Food Hygiene and Safety
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• v.8 no.4
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• pp.215-223
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• 1993

Chloramphenicol (CAP) is a very effective broad-spectrum antibiotic which had been widely used in animal production. However, the drug is not approved in many countries for use in food-producing animals because of its potential toxicity and the possibility of residues in food products. In this study, a modified microbiological assay was developed for the sensitive detection of CAP residues in meat and milk. The method was characterized by the extraction of CAP with ethyl acetate, addition of $0.15\;\mu\textrm{g}$ oxytetracycline/ml in the phosphate buffer diluent (pH 6.0), a luteus ATCC 9341. The lowest levels of CAP detected in muscle tissues and milk were $0.025\;\mu\textrm{g}/ml\;and\;0.05\;\mu\textrm{g}/g$, respectively. Recovery rates free CAP from milk were 68.5%, from bovine muscle 65.1%, from swine muscle 63.8%, and from chicken muscle 59.4%, respectively, and the coefficients of variation were 1.8~15.1%. The results showed that the detection limits of CAP residues in animal products could significantly be improved by the modified microbiological assay than the conventional ones.

• Korean Journal of Microbiology
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• v.42 no.3
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• pp.165-171
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• 2006

ERM proteins transfer the methyl group to $A_{2058}$ in 23S rRNA to confer the resistance to MLS (macrolide-lincosamide-streptogramin B) antibiotics on microorganism ranging from antibiotic producers to pathogens. To define the functional role of peptide segment encompassing amino acid residues 1 to 25 in NTER (N-terminal end region) of ErmSF, one of the ERM proteins, DNA fragment encoding mutant protein deprived of that peptide was cloned and overexpressed in E. coli to obtain a purified soluble form protein to the apparent homogeneity in the yield of 12.65 mg per liter of culture. The in vitro activity of mutant protein was found to be 85% compared to wild type ErmSF, suggesting that this peptide interact with substrate to affect the enzyme activity. This diminished activity of mutant protein caused the delayed expression of antibiotic resistance in vivo, that at fIrst cells expressing mutant protein showed the retarded growth due to the antibiotic action but with time cells inhibited by antibiotic gradually recovered the viability to exert the resistance to the same extent as those with wild type protein.

• Korean Journal of Environmental Agriculture
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• v.32 no.1
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• pp.70-77
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• 2013

BACKGROUND: Nitroxoline is an antibiotic agent. It is used for the treatment of the second bacterial infection by the colibacillosis, salmonellosis and viral disease of the poultry. When the nitroxoline is indiscreetly used, the problem about the abuse of the antibiotics can occur. Therefore, this study presented the residue analytical method of nitroxoline in food for the safety management of animal farming products. METHODS AND RESULTS: A simple, sensitive and specific method for nitroxoline in chicken muscle by high performance liquid chromatograph with PDA was developed. Sample extraction with acetonitrile, purification with SPE cartridge (MCX) were applied, then quantitation by HPLC with C18 column under the gradient condition with 0.1 % tetrabutylammonium hydroxide-phosphoric acid and methanol was performed. Standard calibration curve presented linearity with the correlation coefficient ($r^2$) > 0.999, analysed from 0.02 to 0.5 mg/L concentration. Limit of quantitation in chicken muscle showed 0.02 mg/kg, and average recoveries ranged from 72.9 to 88.1 % in chicken muscle. The repeatability of measurements expressed as coefficient of variation (CV %) was less than 12 % in 0.02 and 0.04 mg/kg. CONCLUSION(S): Newly developed method for nitroxoline in chicken muscle was applicable to food inspection with the acceptable level of sensitivity, repeatability and reproducibility.

• Korean Journal of Veterinary Service
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• v.23 no.1
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• pp.1-8
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• 2000

This study was carried out to simultaneous determination of penicillin G and chloramphenicol in livestock products by HPLC. The results obstained were as follows; 1. Penicillin G and chloramphenicol were analyzed by HPLC on symmetry $C_{18}$ column with acetonitrile-0.1 M phosphate buffer containing 0.0157 M thiosulfate (25 : 75) as mobile phase at UV 325nm and 280nm, respectively. 2. Samples were applied to a SeP-Pak $C_{18}$ cartridge, from which eluted penicillin derivatized with 2 M 1,2,4-triazole containing 0.001 M mercuric chloride. 3. The average recovery rates of penicillin G and chloramphenicol were 81.8% and 80.3%, respectively, and the detection limits were 5 ppb (5$\mu\textrm{g}$/kg: 7.9IU/kg) for penicillin G and chloramphenicol in porcine and bovine muscle.

• Korean Journal of Veterinary Research
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• v.49 no.2
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• pp.135-139
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• 2009

Streptomyces (S.) fradiae is a microbe with broad-spectrum antimicrobial activity, isolated from soil. In the present study, antibacterial effects of S. fradiaea against Salmonella (S.) gallinarum was determined. S. fradiae inhibited growing of S. gallinarum in Luria-Bertani media agar. Moreover, ingestion of S. fradiae markedly inhibited mortality of chickens experimentally infected with S. gallinarum. There is no side effect by S. fradiaeon, in safety of chickens and antibiotic material residues in chicken meat. Taken together, S. fradiae have the antibacterial effects against S. gallinarum. Therefore, we concluded that S. fradiae might be a good microbial candidate for treatment or control of fowl typhoid in chickens.

• BMB Reports
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• v.53 no.12
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• pp.611-621
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• 2020

Bacterial endoribonuclease toxins belong to a protein family that inhibits bacterial growth by degrading mRNA or rRNA sequences. The toxin genes are organized in pairs with its cognate antitoxins in the chromosome and thus the activities of the toxins are antagonized by antitoxin proteins or RNAs during active translation. In response to a variety of cellular stresses, the endoribonuclease toxins appear to be released from antitoxin molecules via proteolytic cleavage of antitoxin proteins or preferential degradation of antitoxin RNAs and cleave a diverse range of mRNA or rRNA sequences in a sequence-specific or codon-specific manner, resulting in various biological phenomena such as antibiotic tolerance and persister cell formation. Given that substrate specificity of each endoribonuclease toxin is determined by its structure and the composition of active site residues, we summarize the biology, structure, and substrate specificity of the updated bacterial endoribonuclease toxins.

• Journal of Applied Biological Chemistry
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• v.57 no.3
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• pp.189-196
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• 2014

In Korea, over 4,700 animal carcass disposal sites were installed until 2011 due to the outbreak of foot and mouth disease. Due to the putrefaction of buried animals, the leachate containing veterinary antibiotics may release into surrounding environments. Antibiotic residues in the environment cause the formation of antibiotic resistance bacteria threatening human and ecosystem health. This study reports the concentrations of five antibiotics, including tetracycline (TC), chlortetracycline (CTC), oxytetracycline (OTC), sulfamethazine (SMZ), and sulfamethoxazole (SMX), in soils from animal carcass disposal site and adjacent agricultural field. Concentrations of antibiotics at animal carcass disposal sites (TC: $144.26-350.73{\mu}g/kg$, SMZ: $17.72-44.94{\mu}g/kg$) were higher than those at agricultural field (TC: $134.16-320.73{\mu}g/kg$, SMZ: $6.48-8.85{\mu}g/kg$) whereas the concentrations of CTC, OTC, and SMX were below detection limit in both sites. Results showed that the antibiotics in animal carcass site might leach to the soil and possibly contaminating the groundwater. Future studies will focus on the transfer of antibiotics residues into food crops.

• Bulletin of the Korean Chemical Society
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• v.32 no.8
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• pp.2577-2583
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• 2011

We have designed a 20-residue hybrid peptide CA(1-8)-MA(1-12) (CAMA) incorporating residues 1-8 of cecropin A (CA) and residues 1-12 of magainin 2 (MA) with high bacterial cell selectivity. CAMA-P2 is an ${\alpha}$-helical antimicrobial peptide designed from a CAMA hybrid peptide and substitution of Gly-Ile-Gly hinge sequence of CAMA to Pro influences the flexibility at central part of CAMA. Based on structure-activity relationships of CAMA peptides, to investigate the effects of the total positive charges on antimicrobial activity of CAMA-P2, the $Ser^{14}{\rightarrow}$Lys analogue (CAMA-syn1) was synthesized. The role of tryptophan at C-terminal ${\alpha}$-helix on its antimicrobial activity as well as synergistic activity was also investigated using $Ser^{14}{\rightarrow}$Lys/$Phe^{18}{\rightarrow}$Trp analogue (CAMA-syn2). Also, we designed CAMA-syn3 by substitution of $Lys^{16}$ located opposite side of substituted $Lys^{14}$ of CAMA-syn1 with Leu residue, resulting in increase of hydrophobicity and amphipathicity of the peptide. All of CAMA-syn analogues showed good antimicrobial activities similar to those of CAMA and CAMA-P2. The CAMA-syn1 and CAMA-syn2 showed low hemolytic activity and cytotoxicity against human keratinocyte Haca-T cells while CAMA-syn3 showed hemolytic activity and cytotoxicity at its MIC value. We then investigated their abilities to act synergistically in combination with the antimicrobial flavonoids and synthetic compounds screened in our laboratory. The results showed that all peptides exhibited synergistic effects with dihydrobinetin, while only CAMA-syn2 exhibited synergistic effects with YKAs3001 against both S. aureus and MRSA, suggesting that Trp residue at C-terminus of CAMA-syn2 may facilitate the polar antibiotic flavonoids and synthetic compounds to permeabilize the membrane. This study will be useful for the development of new antibiotic peptides with potent antimicrobial and synergistic activity but without cytotoxicity.

• BMB Reports
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• v.43 no.5
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• pp.362-368
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• 2010

Dermcidin is a human antibiotic peptide that is secreted by the sweat glands and has no homology to other known antimicrobial peptides. As an initial step toward understanding dermcidin's mode of action at bacterial membranes, we used homonuclear and heteronuclear NMR to determine the conformation of the peptide in 50% trifluoroethanol solution. We found that dermcidin adopts a flexible amphipathic $\alpha$-helical structure with a helix-hinge-helix motif, which is a common molecular fold among antimicrobial peptides. Spin-down assays of dermcidin and several related peptides revealed that the affinity with which dermcidin binds to bacterial-mimetic membranes is primarily dependent on its amphipathic $\alpha$-helical structure and its length (>30 residues); its negative net charge and acidic pI have little effect on binding. These findings suggest that the mode of action of dermcidin is similar to that of other membrane-targeting antimicrobial peptides, though the details of its antimicrobial action remain to be determined.