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갓김치에서 분리한 캡사이신-내성 세균,Leuconostoc mesenteroides GK-10의 생리활성
김유진,나예린,이현호,오계헌 순천향대학교 기초과학연구소 2021 순천향자연과학연구 논문집 Vol.27 No.1.2
The aim of this work was to investigate the physiological activities of capsaicin-resistant bacterium, Leuconostoc mesenteroides GK-10 isolated from fully fermented mustard leaf kimchi. Initially, the morphological, physiological and biochemical characteristics of strain GK-10 were examined. Based on phylogenetic analysis using 16S rRNA sequencing, the isolate was identified as L. mesenteroides GK-10 and phylogenetic tree of the strain was plotted. L. mesenteroides GK-10 grew well in the different concentrations of capsaicin (0-600 μg/mL). Various physiological activities (e.g., tyrosinase inhibitory activity, ACE inhibitory activity, antioxidant activity, SOD-like activity, depletion of sodium nitrite) of L. mesenteroides GK-10 cultures with different concentrations of capsaicin were evaluated and compared to the cultures of L. mesenteroides DK-3 as a standard strain. According to the results, all of the physiological activities evaluated in this work were considerably higher in L. mesenteroides GK-10 cultures with 600 μg/mL capsaicin compared to L. mesenteroides DK-3 cultures with the same capsaicin concentration, although the physiological activities of GK-10 were higher or lower compared to those of DK-3 in the absence of capsaicin. In consequence, this work showed that L. mesenteroides GK-10 strains can maintain their physiological activities despite the presence of high concentrations of capsaicin.
Pheochromocytoma Presenting with Multiple Cardiovascular Manifestations
Yu Na Kim,Cheol Woong Yu,Young Soo Oh 이화여자대학교 의과학연구소 2014 EMJ (Ewha medical journal) Vol.37 No.2
Iintroduction 1 Case 1 Discussion 4 References 5
Na Young Jin,Mi Jin Jeon,You Kyoung Lee,San Na Oh,Mi Ja Seo,Young Nam Youn,Yong Man Yu 한국응용곤충학회 2013 한국응용곤충학회 학술대회논문집 Vol.2013 No.04
Bacillus thuringiensis (Bt) is a gram-positive bacterium that produces parasporal crystal proteins known as endotoxins or Cry proteins. The Cry protoxins are then cleaved by insect midgut proteinases to form active Bt toxins. The activated Cry protein then binds to specific receptors at the midgut epithelium. Cadherin-like and aminopeptidase N (APN) proteins are involved in Bt toxin binding by interacting sequentially with different toxin structures. Aminopeptidase N (APNs) from several insect species have been shown to be putative receptors for these toxins. We have characterized four different midgut APNs(APN1, APN2, APN3, APN4) cDNAs from S. exigua. Forward primers and reverse primers for confirmation of four different midgut APNs were designed based on their sequences cloned from the cDNA libraries. Quantitative RT-PCR procedures includes 42℃ for 20min (cDNA synthesis), 99℃ for 5min, and 35 cycles (94℃ for 1min, and 60℃ for 50 s) for collection. Four aminopeptidase N isoforms were confirmed with qRT-PCR. Sequence analysis was performed by BlastX search the National Center for Biotechnology Information(NCBI) nucleotide. Furthermore, double-stranded RNAs(dsRNAs) were synthesized. DsRNAs were determined for bioassay.