• The Korean Journal of Pain
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• 제28권1호
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• pp.4-10
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• 2015

Etifoxine (etafenoxine, $Stresam^{(R)}$) is a non-benzodiazepine anxiolytic with an anticonvulsant effect. It was developed in the 1960s for anxiety disorders and is currently being studied for its ability to promote peripheral nerve healing and to treat chemotherapy-induced pain. In addition to being mediated by $GABA_A{\alpha}2$ receptors like benzodiazepines, etifoxine appears to produce anxiolytic effects directly by binding to ${\beta}2$ or ${\beta}3$ subunits of the $GABA_A$ receptor complex. It also modulates $GABA_A$ receptors indirectly via stimulation of neurosteroid production after etifoxine binds to the 18 kDa translocator protein (TSPO) of the outer mitochondrial membrane in the central and peripheral nervous systems, previously known as the peripheral benzodiazepine receptor (PBR). Therefore, the effects of etifoxine are not completely reversed by the benzodiazepine antagonist flumazenil. Etifoxine is used for various emotional and bodily reactions followed by anxiety. It is contraindicated in situations such as shock, severely impaired liver or kidney function, and severe respiratory failure. The average dosage is 150 mg per day for no more than 12 weeks. The most common adverse effect is drowsiness at the initial stage. It does not usually cause any withdrawal syndromes. In conclusion, etifoxine shows less adverse effects of anterograde amnesia, sedation, impaired psychomotor performance, and withdrawal syndromes than those of benzodiazepines. It potentiates $GABA_A$ receptor-function by a direct allosteric effect and by an indirect mechanism involving the activation of TSPO. It seems promising that non-benzodiazepine anxiolytics including etifoxine will replenish shortcomings of benzodiazepines and selective serotonin reuptake inhibitors according to animated studies related to TSPO.

• 한국식생활문화학회지
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• 제34권6호
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• pp.785-792
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• 2019

This study examined the changes in the protein and mineral composition of Gryllus bimaculatus fermented with Bacillus substilis and the mycelia of Basidiomycetes. Normal Gryllus bimaculatus (S) and experimental group data obtained after an inoculation of Bacillus substilis (SC) (KACC 19623), Pleurotus eryngii (SP) and Cordyceps millitaris (SC) were compared. The crude protein content of the Gryllus bimaculatus (control) was 75.48%, but it decreased to 64.55, 54.32, and 63.53% after fermentation with SB, SP and SC, respectively (p<0.05). An analysis of the organic elements showed that the contents of the carbon and nitrogen sources were also reduced after fermentation, and the most significant decrease was observed after fermentation with SP. In SDS-PAGE, a 120 kDa and a 48 kDa protein of Gryllus bimaculatus were found. On the other hand, protein bands faded after fermentation with SP and SC, respectively. Moreover, no visible band was observed after fermentation with SB. According to amino acid analysis, the total free amino acid content increased 3.84 and 1.74 times after fermentation with SB and SP, respectively, compared to the corresponding baseline data. In contrast, it decreased by 0.52 times after fermentation with SC. Among the essential amino acids found in crickets fermented with SB, the valine and isoleucine content was 3.57 and 2.64 times higher, respectively, than the recommended daily amount of essential amino acids.

• 공업화학
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• 제24권1호
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• pp.18-23
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• 2013

본 연구는 가자미껍질에서 콜라겐 펩타이드 파우더(FSCP)를 제조하여 시판 틸라피아비늘 유래 콜라겐 펩타이드 파우더 (TSCP)와 이화학적 특성을 비교 검토하였다. FSCP의 물리적인 특성 및 영양성분은 TSCP와 유사하게 나타났으며, 열량에 있어서도 FSCP는 3.82 kcal로 TSCP의 3.84 kcal와 차이가 없는 것으로 나타났다. 아미노산 조성은 FSCP가 TSCP보다 aspartic acid, serine, histidine, tyrosine, methionine의 경우 높았으나, hydroxyproline, proline, alanine은 오히려 낮았다. 특히 필수아미노산 함량은 FSCP가 22.74%로, TSCP의 13.64%보다 높았다. 분자량 분포는 FSCP가 1000 Da으로, TSCP에 비하여 비교적 낮은 분포를 보이고, 유화성 및 유화안정성은 FSCP와 TSCP가 유사한 경향으로 우수하였다.

• 생명과학회지
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• 제11권5호
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• pp.423-431
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• 2001

Agrobacterium에 의한 식물형질전환은 가장 일반적으로 많은 사용되는 식물형질전환 기술이냐 이 과정에서 관여하는 식물 유전자들에 대한 관여하는 식물 유전자들에게 대한 연구는 거의 전무한 상태다. 본 연구는 Agrobacterium의 감염에 저항성을 보이는 새로운 돌연변이들의 분리와 분석 연구에 연속하여 Agrobacterium에 의한 식물형질전환에 관여하는 Arabidopsis RAT3 유전자의 cDNA와 gemonic clone을 plasmid rescue 기술을 이용하여 분리하였다. 염기서열 분석결과, 매우 유사한 2개의 유전자가 (RAT3-1과 RAT3-2)약 600bp 간격을 두고 연속하여 존재함을 밝혔다. 그중 RAT3-1 이 mutagen으로 사용된 T-DNA에 의해 손상을 받아 rat3 돌연변이 형질이 유도되었다. RAT3 유전자의 단백질의 분자량은 15 kDa 정도이며 아미노 밀단에 분비를 위한 signal peptide를 가지며 단백질이 전체적인 매우 친수성인 것으로 미루어 세포막 밖으로 분비될 것으로 생각된다. 이들 유전자의 정확한 생물학적 기능에 대한 연구들이 수행 중이며, 이러한 기초연구는 식물형질전환 기술의 개발에 기여할 것이다.

• 한국축산식품학회지
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• 제37권1호
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• pp.29-37
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• 2017

Defatted bovine liver (DBL) is a potential source of protein and minerals. Supercritical carbon dioxide ($SC-CO_2$) and a traditional organic solvent method were used to remove lipid from bovine liver, and the quality characteristics of a control bovine liver (CBL), bovine liver defatted by $SC-CO_2$ ($DBLSC-CO_2$) at different pressures, and bovine liver defatted by organic solvent (DBL-OS) were compared. The $DBLSC-CO_2$ samples had significantly higher (p<0.05) protein, amino acid, carbohydrate, and fiber contents than CBL and DBL-OS. There was a higher yield of lipid from CBL when using $SC-CO_2$ than the organic solvent method. SDS-PAGE analysis demonstrated that the CBL and $DBLSC-CO_2$ had protein bands of a similar intensity and area, whereas DBL-OS appeared extremely poor bands or no bands due to the degradation of proteins, particularly in the 50 to 75 kDa and 20 to 25 kDa molecular weight ranges. In addition, $DBLSC-CO_2$ was shown to have superior functional properties in terms of total soluble content, water and oil absorption, and foaming and emulsification properties. Therefore, $SC-CO_2$ treatment offers a nutritionally and environmentally friendly approach for the removal of lipid from high protein food sources. In addition, $SC-CO_2$ may be a better substitute of traditional organic solvent extraction for producing more stable and high quality foods with high-protein, fat-free, and low calorie contents.

• 생명과학회지
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• 제18권3호
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• pp.350-356
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• 2008

가지 열매로부터 neutral saline에 의한 추출, $(NH_4)_2SO_4$ 침전 및 Sephadex-G100을 이용한 affinity chromatography에 의해 분리한 lectin의 생화학적 특성을 연구하였다. Trypsin을 처리하지 않은 사람, 쥐와 토끼의 적혈구에서는 혈구 응집반응이 일어나지 않았으며, Trypsin을 처리한 사람, 쥐와 토끼의 적혈구 중에서는 쥐의 적혈구에서만 혈구 응집반응이 일어났다. SDS-PAGE에 의해 가지 lectin의 분자량을 확인한 결과, 19.3 kDa의 단일 band 임이 확인되었다. D-glucose를 포함하는 7개의 탄수화물은 100 mM 이하의 농도에서 lectin과 적혈구의 응집을 저해시키지 않았으므로, 탄수화물에 대한 특이성이 나타나지 않았다. 최적 반응온도 범위는 $10-20^{\circ}C$로서, $20-70^{\circ}C$에서 열에 대해 안정하였으며, 안정된 pH 범위는 pH 6.2-7.2로 확인되었다. $Ca^{2+},\;Co^{2+},\;Cu^{2+},\;Fe^{2+},\;Mg^{2+}$ 및 $Mn^{2+}$ 20 mM 이하의 농도에서는 lectin과 적혈구의 응집을 저해시키지 않았으므로, 금속이온에 대한 특이성이 나타나지 않았다

• Journal of Microbiology
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• 제44권2호
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• pp.185-191
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• 2006

The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH $(5.0{\sim}9.0)$, and remained stable over a broad temperature range $(20^{\circ}C{\sim}60^{\circ}C)$. It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19 % of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50 % at concentrations of $11.5{\mu}M,\;0.52{\mu}M,\;and\;0.11{\mu}M$, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase.

• 한국식품과학회지
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• 제38권2호
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• pp.304-308
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• 2006

본 연구에서는 시판되고 있는 카제인 나트륨, 유청 단백질 분리물, 탈지분유 및 전지분유에 TGase를 첨가하여 단백질 이동특성 및 pepsin에 의한 가수분해 정도를 조사하였다. 우유 단백질과 분말 제품들을 TGase로 2시간 동안 반응시킨 후 전기영동을 실시한 결과 모든 시료에서 고분자량의 중합체를 형성하였으며 가교결합 정도는 카제인 나트륨 >탈지분유 >전지분유 >유청 단백질 분리물 순으로 감소하는 양상을 보였다. 인체 내 소화효소인 pepsin에 의하여 가수분해된 카제인 나트륨은 10kDa 이하의 펩타이드로 분해됐고, 유청 단백질은 분해 전, 후 양상이 유사하였다. 유청 단백질 중 ${\beta}-Lg$는 pepsin에 의해 거의 분해되지 않고 저항성을 보였다. 탈지분유, 전지분유 역시 더 낮은 분자량의 펩타이드가 관찰되었는 바, in vitro 상에서의 TGase작용으로 인한 교차결합은 소화효소에 의한 가수분해가 용이함을 확인하였다. 이 결과는 TGase를 첨가하여 새로운 유제품을 개발, 이용하는데 인체내에서의 소화에 거의 문제가 없을 것임을 시사하는 것으로 보인다.

• 한국해양공학회:학술대회논문집
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• 한국해양공학회 2002년도 추계학술대회 논문집
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• pp.341-346
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• 2002

In this study, an effect that compressive residual stress formed by shot-peening the surface of spring steel(JISG SUP-9) at each shot velocity(1800, 2200, 2600, 3000rpm) on the fatigue crack growth property and threshold stress intensity factor, ${\Delta}K_{th}$, was examined. Followings are the result (1) Compressive residual stress on surface of specimen was determined at each -601 MPa(1800rpm), -638 MPa(2200rpm), -587 MPa (2600rpm), -550 MPa(3000rpm) by shot velocity of shot peening and threshold stress intensity factor, ${\Delta}K_{th}$, fatigue crack growth rate, da/dN, on fatigue crack growth is obstructed by the compressive residual stress was determined at each $5.619\;MPa\sqrt{m}$(Un-peening), $8.319\;MPa\sqrt{m}$(1800rpm), $8.797\;MPa\sqrt{m}$(2200rpm), $7.835\;MPa\sqrt{m}$(2600rpm), $7.352\;MPa\sqrt{m}$(3000rpm) (2) Existing compressive residual stress by effect of shot velocity of shot-peening on relation of crack length. a, and number of cycle, N, was 2 times progressed in case of 2200rpm than specimen of Un-peening on fatigue life. And fatigue life was 1.6 times progressed incase of 3000rpm by Over peening. (3) Fatigue life of Material on Paris' law, $da/dN=C({\Delta}K)^m$, that effect of material constant, C, and fatigue crack growth exponent, m, was influenced by effect of. C and m.

• Restorative Dentistry and Endodontics
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• 제42권2호
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• pp.87-94
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• 2017

Objectives: Chitosan has been widely investigated and used. However, the literature does not refer to the shelf life of this solution. This study evaluated, through the colorimetric titration technique and an analysis of dentin micro-hardness, the shelf life of 0.2% chitosan solution. Materials and Methods: Thirty human canines were sectioned, and specimens were obtained from the second and third slices, from cemento-enamel junction to the apex. A 0.2% chitosan solution was prepared and distributed in 3 identical glass bottles (v1, v2, and v3) and 3 plastic bottles (p1, p2, and p3). At 0, 7, 15, 30, 45, 60, 90, 120, 150, and 180 days, the specimens were immersed in each solution for 5 minutes (n = 3 each). The chelating effect of the solution was assessed by micro-hardness and colorimetric analysis of the dentin specimens. 17% EDTA and distilled water were used as controls. Data were analyzed statistically by two-way and Tukey-Kramer multiple comparison (${\alpha}=0.05$). Results: There was no statistically significant difference among the solutions with respect to the study time (p = 0.113) and micro-hardness/time interaction (p = 0.329). Chitosan solutions and EDTA reduced the micro-hardness in a similar manner and differed significantly from the control group (p < 0.001). Chitosan solutions chelated calcium ions throughout the entire experiment. Conclusions: Regardless of the storage form, chitosan demonstrates a chelating property for a minimum period of 6 months.