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Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified by liquid chromatography-electrospray ionization quantitative time-of-flight mass spectrometry analysis. Of the 28 peptides identified, 11 and 16 were identified as β-casein (CN) and αs1-CN, respectively. One peptide was identified as κ-CN. Three peptides, YQEPVLGPVRGPFPIIV, QEPVLGPVRGPFPIIV, and GPVRGPFPIIV, from β-CN corresponded to known antihypertensive peptides. We also found 15 peptides that were identified as potential antihypertensive peptides because they included a known antihypertensive peptide fragment. These peptides were as follows: RELEELNVPGEIVE (f1-14), YQEPVLGPVRGPFP (f193-206), EPVLGPVRGPFPIIV (f195-206), PVLGPVRGPFPIIV (f196-206), VLGPVRGPFPIIV (f197-206), and LGPVRGPFPIIV (f198-206) for β-CN; and APSFSDIPNPIGSENSEKTTMPLW (f176-199), SFSDIPNPIGSENSEKT- TMPLW (f178-199), FSDIPNPIGSENSEKTTMPLW (f179-199), SDIPNPIGSENSEKTTMPLW (f180-199), DIPNPIGSENSEKTTMPLW (f181-199), IPNPIGSENSEKTTMPLW (f182-199), PIGSENSEKTTMPLW (f185-199), IGSENSEKTTMPLW (f186-199), and SENSEKTTMPLW (f188-199) for αs1-CN. From these results, B. longum could be used as a starter culture in combination with other lactic acid bacteria in the dairy industry, and/or these peptides could be used in functional food manufacturing as additives for the development of a product with beneficial effects for human health.
Milk proteins have many potential sequences within their primary structure, each with a specific biological activity. In this study, we compared and investigated the bioactivities of hydrolysates of the domestic (A, B) and imported (C, D) skim milk powders generated using papain digestion. MALDI-TOF analysis revealed that all milk powder proteins were intact, indicating no autolysis. Electrophoretic analysis of hydrolysates showed papain treatment caused degradation of milk proteins into peptides of various size. The antioxidant activity of the hydrolysates, determined using 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and total phenolic contents (TPC) assays, increased with incubation times. In all skim milk powders, the antioxidant activities of hydrolysates were highest following 24 h papain treatment (TPC: A, 196.48 µM GE/L; B, 194.52 µM GE/L; C, 194.76 µM GE/L; D, 163.75 µM GE/L; ABTS: A, 75%; B, 72%; C, 72%; D, 57%). The number of peptide derived from skim milk powders, as determined by LC-MS/MS, was 308 for A, 283 for B, 208 for C, and 135 for D. Hydrolysate A had the highest antioxidant activity and the most potential antioxidant peptides amongst the four skim milk powder hydrolysates. A total of 4 β-lactoglobulin, 4 αs1-casein, and 56 β-casein peptide fragments were identified as potential antioxidant peptides in hydrolysate A by LC-MS/MS. These results suggest that domestic skim milk could have applications in various industries, i.e., in the development of functional foods.
The nature of encoded information in neural circuits is determined by neuronal firing patterns and frequencies. This paper discusses the molecular identity and cellular mechanisms of spike-frequency adaptation in the central nervous system (CNS). Spike-frequency adaptation in thalamocortical (TC) and CA1 hippocampal neurons is mediated by the Ca2+-activated Cl− channel (CACC) anoctamin-2 (ANO2). Knockdown of ANO2 in these neurons results in increased number of spikes, in conjunction with significantly reduced spike-frequency adaptation. No study has so far demonstrated that CACCs mediate afterhyperpolarization currents, which result in the modulation of neuronal spike patterns in the CNS. Our study therefore proposes a novel role for ANO2 in spike-frequency adaptation and transmission of information in the brain.
Magnetic anomalies are sensitive to magnetic properties present in deep Earth and near surface structures. Such geophysical characteristics often can be quantified by numerical analyses. In this study, we developed a finite element method (FEM) approach to compute magnetic anomalies using COMOL Multiphysics®. This FEM approach was verified by comparing its numerical results with the previously known analytic solution for a uniformly magnetized sphere. Then, we used the method to compute magnetic reversal patterns near mid-ocean ridge with various faulting scenarios. This COMSOL-based approach can be incorporated into advanced multi-physical numerical models to understand the Earth. 지구 자기장은 지구 내부 및 지표면 근처에서 일어나는 다양한 자화 특성 변화에 민감하게 반응하며, 이러한지구물리적 특성은 현장에서 측정된 자기 이상치의 정량적 분석을 통하여 특정화된다. 이 연구에서는 자기 이상치 분석에 활용될 수 있는 유한요소법 기반 수치모델링을 콤솔 멀티피직스를 사용하여 구현하였다. 구현된수치모델링 방법은 기존에 알려진 해석해와 비교하여 그 유효성을 검증하였으며, 중앙해령에서 지자기 역전과단층 구조 사이의 상관관계를 모사하는 데 적용하였다. 이러한 유한요소 기반의 지자기 모델링 기법은 다중 물리적 현상 모사에 손쉽게 적용될 수 있다.
Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical pro-ducts. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethyl-benzothiazoline-6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absor-bance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electro-phoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest val-ues after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation,that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was 87.8µM, whereas 14.5 µM GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORAC-FL assay, antioxidant activity corresponding to 45.7 µM of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.