• Title/Summary/Keyword: 단백질 침착

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Comparisons of Adherence Level of Micro-organisms According to Contact Lens Materials and Protein Deposition and Disinfection Efficacy of Multipurpose Solution (콘택트렌즈 재질 및 침착 단백질에 따른 균 흡착 정도와 다목적용액의 살균력 비교)

  • Sung, Hyung Kyung;Kim, So Ra;Park, Mijung
    • Journal of Korean Ophthalmic Optics Society
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    • v.20 no.1
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    • pp.35-42
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    • 2015
  • Purpose: The present study was aimed to compare the difference in adherence level of microorganisms according to contact lens materials and protein deposition and to evaluate disinfection efficacy of multipurpose solution. Methods: The evaluations of micro-organisms' adherence and disinfection efficacy of multi-purpose solution were conducted by employing the Part 2. Regimen Procedure for Disinfecting Regiments in the Disinfection Efficacy Testing under the "FDA Evaluation Criteria & Method". Results: Pseudomonas aeruginosa, Serratia marcescens, Candida albicans except Staphylococcus aureus adhered more on etafilcon A lens and disinfection efficacy of total 4 products investigated was almost perfect except Candida albicans. The 3 micro-organisms except Serratia marcescens adhered more to albumin-predeposited lens. Disinfection efficacy of multi-purpose solution was higher against the micro-organisms adhered to albumin-deposited lens than against the micro-organisms adhered to the lysozyme-deposited lens. Furthermore, disinfection efficacy of multi-purpose solution was different according to types of micro-organisms. Conclusions: It was revealed that the type of micro-organisms, the lens materials and type of absorbed tear protein affected the amount of adhered micro-organisms to contact lens and that adhesion of tear protein could induce the change of disinfection efficacy of multi-purpose solution. It suggest that the hygienic condition of contact lens can vary by these factors influencing on disinfection efficacy and the occurrence of adverse effect can be affected.

The Change in the Amounts of Proteins and Lipids Deposited on Soft Contact Lens Caused by Drinking (음주로 인한 소프트콘택트렌즈의 단백질 및 지질 침착양 변화)

  • Kim, So Ra;Lim, Shin Gyu;Bae, Seok Chun;Choi, Jung Hyun;Park, Sang Hee;Park, Mijung
    • Journal of Korean Ophthalmic Optics Society
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    • v.17 no.2
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    • pp.233-239
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    • 2012
  • Purpose: In the study, the change of protein and lipid deposits on soft contact lens by drinking was investigated. Methods: Fifty male subjects wearing soft contact lens were surveyed whether they felt any discomfort induced by drinking or not. Further, 32 male subjects who has no ocular disease drank 190 mL alcohol. The protein and lipid deposits on soft contact lens (etafilcon A material) of subjects were measured after 4 hours later and compared with those of non-drinking subject. Results: When subjects drink alcohol with soft contact lens on, 58% of subjects answered they experienced the change of lens awareness such as stiffness, blurry sight, dryness and so on. The protein deposit on soft contact lens increased an average of $59.3{\mu}g/lens$ by drinking and the case of more than double in protein deposit was reached in 9 eyes. However, the protein deposited on soft contact lens was lysozyme which was unchanged by drinking. The amounts of cholesterol and methyl oleate after drinking were 85.5% (p=0.25) and 52.6% (p=0.002) of non-drinking's indicating some change of lipid deposit on soft contact lens by drinking. Conclusions: The results showed the composition of protein and lipid deposited on soft contact lens was changed due to drinking. Thus, it is suggested that wearing soft contact lens when drinking might be one of the reasons to feel discomfort.

The Change in Refractive Powers of Soft Contact Lenses Caused by the Deposition of Tear Proteins (누액 단백질 침착에 의한 소프트콘택트렌즈의 굴절력 변화)

  • Choi, Jin-Yong;Park, Jae-Sung;Kim, So Ra;Park, Mijung
    • Journal of Korean Ophthalmic Optics Society
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    • v.16 no.4
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    • pp.383-390
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    • 2011
  • Purpose: The present study was conducted to investigate whether refractive powers of soft contact lenses were induced by the deposition of tear proteins when wearing soft contact lenses. Methods: The soft contact lenses (material: etafilcon A, hilafilcon A and comfilcon A) with refractive powers of -1.00 D, -3.00 D, -5.00 D and -7.00 D were incubated in artificial tear for 1 day, 3 days, 5 days, 7 days and 14 days, respectively. After incubation, their refractive powers were measured by wet cell method with an auto-lens meter and their protein deposited on the lenses was determined by the method of Lowry. Results: Among three types of soft contact lenses, the most protein deposition was detected in ionic etafilcon A lens material and significant change of its refractive power was manifested. In other words, refractive powers of etafilcon A lenses firstly decreased after 1 day incubation in artificial tear and then gradually increased with increasing incubation period again. The observed change in refractive powers of all diopters of etafilcon A material was beyond the scope of standard error and bigger in the lens with lower optical power. On the other hand, non-ionic hilafilcon A showed less protein deposition as much as about 20% in etafilacon A and statistically significant increase of refractive powers with increasing incubation period in artificial tear. The change in refractive power of hilafilcon A was also beyond the scope of the standard of error when incubating in artificial tear and greater in the lens with lower diopter. The least protein deposit was shown in silicone hydrogel lens material, comfilcon A as approximately 10% of it in etafilcon A, indicating less change in refractive power within the standard range of error. Conclusions: The large change of refractive powers that was beyond the scope of standard error by the deposition of tear proteins on soft contact lenses was differently detected depending on lens materials in the current study. Thus, the deposition of tear proteins induced by longer period of lens wearing may be one of the causes that induces blurred vision, suggesting that soft contact lens wearers with the amount of tear proteins may need to choose proper lens material.

Adsorption of Salivary Proteins on Titanium Implants (타이태늄 임플란트 표면에 형성된 타액성 단백질에 관한 생체연구)

  • Lee, Seung-Ho;Ku, Yong;Lee, Yong-Moo;Rhyu, In-Cheol;Chung, Chong-Pyoung;Han, Soo-Boo;Choi, Sang-Mook
    • Journal of Periodontal and Implant Science
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    • v.33 no.2
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    • pp.127-137
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    • 2003
  • 치과용 임플란트 실패의 주요 원인은 임플란트 표면에 부착되는 세균의 침착의 결과로 생기는 임플란트 주위염이다. 구강 내에서 세균성 치태의 침착은 치태가 부착하는 기질 표면의 물리적 성상과 타액성 피막의 성분에 영향을 받으며 형성된 피막의 유기질 성분의 차이가 치태의 성분과 병원성에 영향을 미친다. 최근 연구에 의하면 생체재료의 표면에 침착되는 치태세균은 사용되는 재료에 따라 특이한 세균 침착을 보이며 이는 초기 타액성 피막의 차이에 의한 것으로 알려져 있다. 이 연구의 목적은 플라즈마분사법으로 표면 처리된 타이태늄 임플란트에 흡착되는 타액성 단백질 피막의 특성을 정성적인 방법으로 분석하는 데 있었다. 법랑질 조각과 플라즈마분사법으로 표면 처리된 타이태늄 임플란트를 스프린트에 치실을 이용하여 연결한 장치를 구강 내 장착하여 2시간 동안 피막이 침착되게 한 후 피막을 분리 추출하여 냉동 건조시켰다. 재수화 과정을 거치고 나서 전기 영동법과 Western transfer 분석을 통해 단백질 성분에 관한 분석을 시행하였다. 사람의 총 타액과 이하선 타액 및 악하선-설하선 타액을 수집기를 이용하여 채취하고 같은 방법으로 처리한 후 성분분석을 실시하였다. 피막 흡착 전후의 표면변화를 주사전자현미경을 이용하여 관찰하였다. 실험결과 타이태늄 임플란트에 흡착된 피막은 법랑질 표면의 피막과는 다른 단백질 성분을 가지고 있었으며, 주로 악하선-설하선 타액에서 유래하였다. 임플란트와 법랑질 표면 모두에서 흡착된 피막에는 아밀라제, 분비성 면역 글로불린A 및 락토페린이 존재함을 알 수 있었으나 법랑질의 경우는 blotting이 약하게 나타났다. 주사전자현미경 관찰결과 시편의 표면에 균질한 피막이 덮고 있었으며 세균의 부착은 거의 관찰되지 않았다. 이상의 실험 결과들을 통하여 플라즈마분사법으로 표면 처리된 타이태늄 임플란트 표면에 부착된 타액성 단백질 성분은 법랑질과는 차이가 있음을 알 수 있었으며, 이러한 차이는 치태세균의 종류 및 병원성에 영향을 미칠 것으로 생각된다. 법랑질과 타이태늄 임플란트는 기질과 표면구조가 다르므로 표면에 형성 되는 치태성분도 다르다는 사실과 본 연구 결과를 종합하여 볼 때, 타이태늄 임플란트 표면에 흡착되는 초기 타액성 단백질의 성불이 타이태늄 표면에 침착되는 미생물 군의 조절에 중요한 역할을 가지고 있으며, 임플란트 치료 시에 올바른 치태 관리법의 교육을 통하여 환자 스스로 적절한 관리를 하도록 함으로써 임플란트 치료의 성공률을 높일 수 있을 것으로 생각된다.

The diameter and base curve changes of soft contact Lens by protein deposition (단백질 침착에 의한 소프트콘택트렌즈의 직경 및 곡률반경 변화)

  • Park, Mi-Jung;Cho, Gyu-Tae;Shin, Sung-Hwan;Lee, Heum-Sook;Kim, Dae-Soo
    • Journal of Korean Ophthalmic Optics Society
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    • v.10 no.3
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    • pp.165-171
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    • 2005
  • The aim of the study was to investigate the diameter and base curve changes of soft contact lens by protein deposition. Soft contact lenses were soaked in artificial tear or protein solution which had the same composition with tear for 2min, 10min, 30min, 1hr, 3hr, 6hr, 12hr, and 24hr. Diameter and base curve changes of soft contact lenses were examined by using the high speed camera(Fastcam ultima 1024). The longer the soaking time of soft contact lenses in the artificial tear, the diameter and base curve changes of soft contact lenses was more increased. In the case of soft contact lenses adsorbed only protein, the similar pattern was shown and the diameter and base curve were decreased. However, the influence of calcium ion was found to be less than that of protein. These results suggest that the tear protein causes the diameter and base curve decrease of soft contact lens, which might be related to the discomfort after soft contact lens wearing.

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Experimental Study on the Prevention of Periodontal Disease (치주질환 발생기전 및 예방에 관한 실험적 연구)

  • Choi, Keun-Bai
    • The Journal of the Korean dental association
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    • v.17 no.12 s.127
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    • pp.895-899
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    • 1979
  • 치석다침착자의 치석의 화학성분함량을 구명하기 위하여 치태제거후 6개월에 치태침착도가 심한 사람과 경한 사람을 분류하여 전악으로부터 치태를 채취하였다. 그리고 채취된 치태 세포성분획과 비세포성 부분으로 분리하여 각 분획에서 탄수화물, 단백질, 지질, Ca, Mg, K 및 P의 함량을 화학적으로 분석측정한 결과는 다음과 같다. 1. 치석다침착자의 치태 건조중량당 10%의 탄수화물, 43%의 단백질, 18%의 지질, 4.3%의 Ca, 0.15%의 Mg, 0.29%의 K과 2.87%의 P으로 구성되어 있다. 2. 탄수화물, 지질, K은 비세포 성분획에서 단백질, Mg, 세포성분획에서 많이 차지하였다. 3. Ca, Mg, P의 함량은 치석다침착자의 치태에서 K의 함량은 치석경침착자의 치태에서 높았다. 4. Ca/P비는 비세포성분획보다 세포성 분획에서 훨씬 낮았다.

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Analysis of Evaluation Methods for the Efficacy of Protein Removal Agents for Soft Contact Lens (소프트콘택트렌즈 단백질제거제의 효능 평가법 분석)

  • Byuna, Hyun Young;Sung, Hyung Gyeong;Won, Hye Lim;Shim, Ji In;Park, Mijung;Kim, So Ra
    • Journal of Korean Ophthalmic Optics Society
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    • v.19 no.1
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    • pp.51-57
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    • 2014
  • Purpose: The present study was conducted to establish the experimental condition for the proper evaluation of protein removal efficacy when developing protein removal agents. Its protein removal efficacy was further analyzed and compared with the result from protein removal efficacy against protein deposition on contact lens to suggest the evaluation method for efficacy of protein removal agents. Methods: Protein digestibility assay presented in the Korean pharmacopoeia was selected to establish the evaluation method for efficacy of papain, pancreatin, subtilisin A and protease itself as a ingredient and protein removal tablets or solution containing those enzymes and find a suitable test conditions. Furthermore, the cleaning efficacy of commercially available protein removal tablets and solution on balafilcon A lens deposited with protein artificially was measured and the correlation between two evaluation methods was further analyzed. Results: When pancreatin itself and the product containing pancreatin was evaluated by protein digestibility assay, both reached 28 IU/mg, the standard value of protein digestibility suggested by the Korean pharmacopoeia. In case of protease and subtilisin A tested with trichloroacetic acid B solution, both of them met the enzyme activity level proposed by the manufacturers when they were evaluated by protein digestibility assay however, papain and subtilisin A tested with trichloroacetic acid A solution were not reached the enzyme activity level. Among protein removal agents, three products except a product containing pancreatin did not meet the enzyme activity value specified by the manufacturer when they were evaluated by protein digestibility assay. However, actual protein removal efficacy of three products except a papain-containing product on the lens was greater than 90% protein removal. In the case of papain-containing protein removal product, its effect was not measured by protein digestibility assay however, its actual protein removal efficacy on the lens reached 73.72%. Conclusions: From the results, it was confirmed that the efficacy of protein removal agents for contact lens should be evaluated by different method according to the type of proteolytic enzyme contained. That is, the protein removal agents containing pancreatin, protease and subtilisin A can be evaluated by protein digestibility assay and protein removal efficiency evaluation and the products containing papain can be effectively evaluated by only the evaluation method for protein removal efficiency employing the lens.

The Evaluation of Property of Colored Contact Lenses (칼라콘택트렌즈의 물성적 특성 평가)

  • Park, Hyun-Ju
    • Journal of Korean Ophthalmic Optics Society
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    • v.10 no.2
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    • pp.119-126
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    • 2005
  • The purpose of this study was analyzed to compare on the physical characters of two companies of color contact lenses. Artificial tear solution was used for measuring the rate of protein deposits and wettability. The surface roughness of lenses was measured by SEM(scanning electron microscope, Japan) and AFM(atomic force microscope, MultimodeTM, USA). As a results, The color contact lenses was not different from general soft contact lenses in a respect of other properties. However, the colored contact lenses showed a severe crack on the surface under SEM observation. There was no irregularity on the surface of the colored contact lenses in AFM photograph. The dyes were deposited in inside of lenses by microscope observation.

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Dystrophin Degradation in Skeletal Muscles with Lipid Enrichment in Cattle (지방 침착률이 높은 식용소에서 나타난 골격근의 디스트로핀 소실)

  • Jeon, Sung-Hwan;Kim, Ah-Young;Lee, Eun-Mi;Lee, Eun-Joo;Hong, Il-Hwa;Hwang, Ok-Kyung;Jeong, Kyu-Shik
    • Journal of Life Science
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    • v.26 no.5
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    • pp.592-602
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    • 2016
  • This study investigated the muscular dystrophin levels in freely moving Australian cattle mainly fed grass, freely moving Korean cattle fed mainly a grain diet, and Korean cattle fed a grain diet but housed in a relatively limited space of a cow house. The total skeletal muscle specimens of 244 cattle were collected and immediately fixed in 10% neutral formalin. The same area was biopsied from the cattle in both countries. The findings showed that fatty infiltration is highly correlated with membrane-associated protein degradation in skeletal muscle, and that among several membrane-associated proteins, dystrophin showed the most significant reduction in expression in the cattle with fatty infiltration. Similarly, CD36 was more highly expressed in the cattle with fatty infiltration of skeletal muscle. Various breeding factors, such as oxidative stress; the presence of oxidized lipids in the diet; and environmental factors such as exercise, temperature and amount of time spent, may have critical effects on the degradation of normal cytoskeleton proteins, which are required for maintaining normal skeletal muscle architecture. Among the sarcolemma membrane-associated proteins, dystrophin is the most sensitive membrane protein that is involved muscular dystrophy and muscular degeneration. Thus, the present findings may be useful for studies on muscular dystrophy in humans or the pathogenesis of muscular diseases in animal models.

Separation of Highly Purified Antimicrobial Lysozyme Using Ultrafiltration and Characteristics of Membrane Fouling (한외여과 공정을 이용한 고순도 향균 Lysozyme 의 분리 및 막 침착 특성)

  • Lee, Eun-Young;Woo, Gun-Jo
    • Korean Journal of Food Science and Technology
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    • v.31 no.2
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    • pp.458-464
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    • 1999
  • The value of lysozyme as a natural food preservative is continuously increased due to its unique antimicrobial activity. To determine the optimum separation concentration among the various hen egg white protein (HEWP) concentrations (0.25, 0.5, 1.0, w/v), protein concentrations, lysozyme concentrations, specific activities (SA), and purification factors of prefiltered solution (PFS) and PM30 permeate solution (PMS) were compared. The purity of lysozyme separated at each step was analyzed and confirmed by gel permeation chromatography and electrophoresis. The fouling deposits on membrane were observed by SEM. The non-enzymatic proteins were removed over 99% by ultrafiltration (UF). The increased feed concentration did not contribute to the increase of SA. SA of PMS was 18 to 31 times higher than that of PFS. The optimum feed concentration was decided as 0.25% based on SA and purification factor. The non-enzymatic region of gel chromatogram was proved to be ovalbumin. The thickness of deposit on the UF membrane was approximately $0.9{\mu}m$ and removed by cleaning with 0.1 N NaOH. Therefore, UF using PM30 membrane was very effective to separate the antimicrobial lysozyme from various HEWPs.

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