• 한국식품과학회지
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• 제19권2호
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• pp.89-96
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• 1987

방어와 갈색띠 매물고둥에서 myosin과 paramyosin 을 추출하고, 이들 단백질의 가열중에 일어나는 변성기구를 아미노산 잔기와 SH기의 변화 및 단백질간의 상호작용 등을 측정하므로서 분석하였다. 각 단백질을 이루는 구성아미노산의 측쇄중 소수성 잔기의 유리정도는 가열온도 $65^{\circ}C$까지는 증가하였으나, 그 이상의 가열온도에서는 감소하는 경향을 보였다. 유리 소수성 잔기가 증가하여 감에 따라, 단백질간 상호작용도 활발하여 갔으며, 소수성 잔기의 유리정도가 감소하는 가열온도$65^{\circ}C$부터는 단백질의 응집이 일어나기 시작 하였다. 단백질간의 상호작용을 탁도로써 분석하여 Arrhenius식으로 해석한 결과, 방어 myosin은 3단계이상의 변성과정으로 구분할 수 있었으며, 갈색띠 매물고둥 paramyos은 2단계의 변성과정으로 구분할 수 있었다. 이들 두 단백질 소수성, 용해도, 유리 SH기의 수 및 단백질간의 상호작용 등은 온도함수와 밀접한 상관관계를 보였다.

• 한국축산식품학회지
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• 제41권6호
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• pp.1022-1035
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• 2021

This study estimated the effect of exposure to propiconazole through implementation and residues in finishing pigs. We analyzed the expression of fibrosis-related genes and performed histological analysis of the blood, liver, kidney, muscle, ileum, and fat tissues. The animals were exposed for 28 d to different concentrations of propiconazole (0.09, 0.44, 0.88, 4.41, and 8.82 mg/kg bw/d). Quantitative, gene expression, and histological analyses in tissues were performed using liquid chromatography mass spectrometry, real-time PCR, and Masson's trichrome staining, respectively. Final body weight did not differ among groups. However, genes involved in fibrosis were significantly differentially regulated in response to propiconazole concentrations. Glucose, alanine aminotransferase, and total bilirubin levels were significantly increased compared with those in the control group, while alkaline phosphatase level was decreased (p<0.05) after exposure to propiconazole. The residue limits of propiconazole were increased in the finishing phase at 4.41 and 8.82 mg/kg bw/d. The liver, kidney, and ileum showed blue staining after propiconazole treatment, confirmed by Masson's trichrome staining. In conclusion, these findings suggest that propiconazole exposure disturbs the expression of fibrosis-related genes. This study on dietary propiconazole in pigs can provide a basis for determining maximum residue limits and a better understanding of metabolism in pigs and meat products.

• 한국동물위생학회지
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• 제13권1호
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• pp.21-26
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• 1990

This survey was carried out to determine sulfamethazine residues in urine, kidney and muscle of slaughtered pigs. For this investigation, 20 samples for export and 30 samples for domestic market were collected at slaughterplant in Anyang city from the early of November to the end of December and comparatively were analyzed by SOS test kit and HPLC the results obtained were summarized as follows : 1. Five of 50 samples of swine urine which were inspected by SOS test kit were appeared to sulfamethazine positive 2. The sulfamethazine residue In one of 50 samples of swine muscle was exceeded 0.1ppm 3. The positive samples by SOS test kit were agreed with the results of HPLC quantitative analysis

• 한국초지조사료학회지
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• 제38권3호
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• pp.156-164
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• 2018

Pesticide application in agriculture provides significant benefits such as protection from disease, prevention of harmful insects, and increased crop yields. However, accurate toxicological tests and risk assessments are necessary because of many related adverse effects associated with pesticide use. In this review, we discuss and analyze residual pesticides contained in livestock feed in Korea. A pesticide residue tolerance standard for livestock feed has not been precisely established; so, risk assessments are required to ensure safety. Standards and approaches for animal criteria and appropriate methods for evaluating residual pesticides are discussed and analyzed based on technology related to animal product safety in Korea. The safety of livestock feed containing pesticides is assessed to establish maximum residue limits relative to pesticides. Analysis of residual pesticides in milk, muscle, brain, and fat was performed with a livestock residue test and safety evaluation of the detected pesticide was performed. Efficacy of organic solvent extraction and clean-up of feed was verified, and suitability of the instrument was examined to establish if they are effective, rapid, and safe. This review discussed extensively how pesticide residue tolerance in livestock feed and hazard evaluation may be applied in future studies.

• Bulletin of the Korean Chemical Society
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• 제29권6호
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• pp.1173-1178
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• 2008

A simple and sensitive high-performance liquid chromatographic method was developed for the simultaneous identification of enrofloxacin and its active metabolite ciprofloxacin in chicken muscle. Norflorxacin imprinted polymers synthesized in water-containing systems show high selectivity to enrofloxacin and ciprofloxacin in an aqueous environment. Using these water-compatible imprinted polymers as selective adsorbents in the solid-phase extraction of enrofloxacin and ciprofloxacin from chicken samples, the remaining biological matrix could be quickly washed out from the imprinted column while enrofloxacin and ciprofloxacin were selectively retained and enriched. Analytical separation was performed on a $C_{18}$ column using acetonitrile-water as a mobile phase and fluorescence detection. Good linearity was obtained from 0.8 to 500 ng/g (r > 0.998) with relative standard deviation of less than 3.9%. The mean recoveries of enrofloxacin and ciprofloxacin from chicken muscle were 80.6-94.5% and 77.8-91.8% at three different concentrations. The limits of determinations based on S/N=3 were 0.07 ng/g and 0.09 ng/g, which are below the maximum residue limits established in many countries.

• 대한수의학회지
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• 제47권2호
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• pp.241-245
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• 2007

Parallux (IDEXX Laboratories, USA), a solid-phase fluorescence immunoassay (SPFIA) developed for antibiotics residue detection in milk, was applied for analysis of antibiotics in muscle tissue of olive flounder (Paralichthys olivaceus), rockfish (Sebastes schlegeli), and red sea bream (Pagrus major). Fishes were dipped in streptomycin 20 g/ton water, the recommended therapeutic dose, for 3 consecutive days. Muscle was sampled after 1st, 2nd, 3rd, 4th and 5th day drug treatment. The concentration of streptomycin in muscle, determined by SPFIA, was compared with that of internal standard (200 ppb as streptomycin). The absorbance ratio of sample to internal standard (S/C) was employed as an index to determine the muscle residues in fishes. The standard solutions were added to muscle samples to give final concentrations in muscle of 0.2 and 0.5 mg/ml to investigate the recovery rate. The recovery rates of all spiked samples were > 84% of the spiked value. Streptomycin was detected in muscles of fishes treated after the 1st day of withdrawal period. The present study showed that the SPFIA can be easily adopted in predicting muscle tissue residues for streptomycin in farmed fishes.

• 생명과학회지
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• 제14권5호
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• pp.770-777
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• 2004

a-Tropomyosin (TM)의 아미노(N) 말단 구조의 중요성을 확인하기 위하여 N 말단에 알라닌 아미노산 잔기 하나를 첨가한 재조합 Ala-TM을 제조하였다. Ala-TM을 대장균에서 대량발현 시켜 정제한 후, N 말단이 아세틸화된 근육TM및 N말단에 알라닌-세린 잔기를 첨가한 AS-TM과 N말단이 비아세틸화된 TM등의 재조합 TM과 기능을 비교하였다. Ala-TM은 비아세틸화된 TM보다 액틴친화력이 현저히 증가했으나, 근육 및 AS-TM 보다는 약 3배정도 약하게 액틴에 결합하였다. 근육 TM, AS-TM,그리고 Ala-TM모두가 myosin 51의 농도가 낮을 때 ATPase 활성을 억제하였고 농도가 높을 때 촉진하였으나, 억제와 촉진의 정도는 서로 차이가 있었으며 비아세틸화된 TM은 억제하지 않았다. 이들 결과는 N말단 구조가 TM의 기능을 결정하는 중요한 요소임을 나타내며 TM의 온전한 기능을 위해서는 아세틸화된 N 말단이 필요하다는 것을 의미한다.

• 한국식품위생안전성학회지
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• 제22권1호
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• pp.23-28
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• 2007

Streptomycin을 물 1ton에 20 g을 녹여 넙치, 조피볼락 그리고 참돔을 3일 동안 약욕을 통해 투여한 다음, 휴약기간 동안 근육조직 내 잔류 분포를 조사하였다. 실험어는 해수 중에서 일정한 크기의 케이지에 일반 상업용 사료를 주어 사육하였고, 실험에 사용하기에 앞서 15일 동안 환경에 적응시켰다. 약제 투여 후, 근육시료는 1, 2, 3, 4, 그리고 5일에 각각의 실험어를 대상으로 채취하였다. Streptomycin의 잔류분석은 LC-MS/MS를 이용하여 분석하였다. Streptomycin의 회수율은, 0.05 mg/kg의 농도에서 87.2-102.3%, 0.1 mg/kg의 농도에서는 80.4-94.1%를 보였다. 투약 후 1일에는, 참돔의 근육 중 streptomycin의 잔류농도가 넙치와 조피볼락의 근육 중 잔류농도에 비하여 높았으나 통계적 유의성은 없었으며, 투약 후 2일에는, 모든 근육 시료에서 streptomycin이 검출되지 않았다. 이상의 결과로부터, streptomycin의 약욕을 통한 투여는 넙치, 조피볼락 그리고 참돔의 근육 중에서 안전휴약기간(5일)보다도 체내 소실이 빨리 일어나는 것으로 추정되는 바, 안전휴약기간을 준수한다면 streptomycin의 어류 근육 조직 내 잔류로부터 안전할 것으로 사료된다.

• 한국동물위생학회지
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• 제29권3호
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• pp.317-330
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• 2006

This study was conducted to develop the analytical method about simultaneous determination for synthetic antimicrobials in muscle by high performance liquid chromatography - mass selective detector (HPLC- MSD). Solid phase extraction (SPE), matrix solid phase dispersion (MSPD) and liquid-liquid extraction (LLE) have been adapted as pretreatment procedures for HPLC- MSD. Among various solvent tested, methanol was chosen for extraction of synthetic antimicrobials in muscles. For the optimized response, the values of various MS parameters including fragment voltage, drying gas flow, nebulizer pressure, drying gas temperature were verified. The average recovery rates using MSPD and SPE for muscles of bovine and pork were 78.9-127.1% and 78.3-121.7%, respectively. This method was verified the satisfactory performance for fourteen synthetic antimicrobials excepting carbadox in muscle of pork as detection limit of $0.05{\mu}g/g$ on API/ES SIM mode.

• 한국해양생명과학회지
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• 제3권1호
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• pp.1-8
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• 2018

Myosin is considered as the vital motor protein in vertebrates and invertebrates. Our present study was conducted to decipher the occurrence of myosin in dog fish (Squalus mitsukurii). We isolated one clone containing 979 bp cDNA sequence, which consisted of a complete coding sequence of 453 bp and a deduced amino acid sequence of 150 amino acids from the open reading frame with molecular weight, isoelectric point and aliphatic index are 16.72 Kda, 4.49 and 78.00, respectively. It contained 428 bp long 3' UTR with single potential polyadenylation signals (AATAAA). The predicted EF CA²⁺ binding domains were identified in residue 6-41, 83-118 and 133-150. A BLAST search indicates this protein exhibits a strong similarity to whale shark (Rhincodon typus) MLC3 (91% identical) and also house mouse (Mus musculus) MLC isoform 3f (81% identical). Phylogenetic analysis revealed that this protein is a MLC 3 isoform like protein. This protein also demonstrates highly conserved region with other myosin proteins. Homology modeling of S. mitsukuri was performed using crystal structure of Gallus gallus skeletal muscle myosin II based on high similarity. Reverse transcription-polymerase chain reaction (PCR), quantitative PCR results exhibits dogfish myosin protein is highly expressed in muscle tissue.