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The Purification and Characterization of Bacillus subtilis Tripeptidase (PepT)
Park, Yong-Seek,Cha, Myung-Hoon,Yong, Whan-Mi,Kim, Hyo-Joon,Chung, Il-Yup,Lee, Young-Seek Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.3
A tripeptidase (PepT) was purified to homogeneity from Bacillus subtilis through four sequential chromatographies including DEAE-Sepharose ion exchange, hydroxylapatite, mono-Q FPLC ion exchange, and Superose-12 FPLC gel filtration. The apparent molecular mass of the enzyme was 49,200 Da and 51,400 Da as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography, respectively, and the enzyme exists in a monomeric form. The physicochemical properties of the enzyme were as follows: optimum pH at 7.5, optimum temperature at $60^{\circ}C$, and pI at 4.9. The $K_m$ and $V_{max}$ values of the enzyme were 4.3 mM and 2.5 mmol/min/mg, respectively, with MetAla-Ser as substrate. The B. subtilis PepT requires $Co^{2+}$ ion(s) for activation, while it is inactivated by EOTA and 1,10-phenanthroline, suggesting that it is a metalloprotein. The enzyme was not inhibited by any of serine protease, aspartic protease, or leucine aminopeptidase inhibitors. The enzyme showed comparable activities towards four different substrates including Met-Ala-Ser, Leu-Gly-Gly, Leu-Ser-Phe, and Leu-Leu-Tyr. The amino terminal sequence of PepT determined by Edman degradation was found to be MKEEIIERFTTYVXV and turned out to be identical to that of PepT deduced from a cloned B. subtilis pepT.
Profiling of miRNA expression in mice kidney with diabetic nephropathy
Park, Hye Rim,Lee, Seung Eun,Kim, Hyemi,Jeon, Seeun,Han, Dongkyo,Jin, Young-Ho,Cho, Jeong-Je,Ahn, Hyun-Jong,Park, Cheung-Seog,Lee, Jongsung,Park, Yong Seek THE KOREAN SOCIETY OF TOXICOGENOMICS AND TOXICOPRP 2018 MOLECULAR AND CELLULAR TOXICOLOGY Vol. No.
Yong Seek Park,이승은 셀메드 세포교정의약학회 2013 TANG Vol.3 No.1
The present review investigates the role of the cytoprotective enzyme heme oxygenase-1 (HO-1) in human diseases and explores strategies for its clinical use. In recent years, there has been a growing evidence, for the beneficial effects of some phytoconstituents via induction of HO-1 expression, contained in commonly used spices, fruits, and herbs, in preventing various pathologic conditions, including cancer, diabetes, and cardiovascular diseases. HO-1 catalyzes the rate-limiting step in heme catabolism to generate ferrous iron, carbon monoxide, and biliverdin. HO-1 is reported to play crucial roles in cellular protection, such as anti-inflammatory, anti-proliferative and anti-apoptotic effects. These evidences indicate that HO-1 may functions as a potential therapeutic target in various human diseases. The article highlights the current status of the development of the HO-1 modulation pathway using dietary phytoconstituents.
박용규 ( Park Yong-kyu ),최병걸 ( Choi Byung-keol ),윤주용 ( Yoon Ju Yong ),최상훈 ( Choi Sang-hoon ),윤기원 ( Yoon Gi-won ),이대식 ( Lee Dae-seek ) 한국건축시공학회 2022 한국건축시공학회 학술발표대회 논문집 Vol.22 No.2
This research reviewed the status of binder removal depending on the heating temperature and duration by using the 3D sand mold as an electric heating method. In the case of the electric heating method, it was confirmed that a heating temperature of at least 800℃ or higher was required to remove the binder of the 3D sand mold, and the heating duration was confirmed to be about 10 minutes. Afterwards, it is considered necessary to further evaluate the additional binder removal method and the utilization of recycling silica in consideration of economic feasibility and productivity.