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- 저자 : SeongJooPark (검색결과 3 건)
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Seong-Joo Park,Youn Joung Cho,Ji-Hye Oh,황정원,도상환,Hyo-Seok Na 대한마취통증의학회 2013 Korean Journal of Anesthesiology Vol.65 No.3
Background: We investigated the effects of a magnesium sulfate pretreatment on intubating conditions and cardiovascular responses during rapid sequence tracheal intubation (RSI) in this double-blind randomized study. Methods: Adult patients (n = 154) were randomly allocated to a rocuronium-0.6, rocuronium-0.9, or magnesium group. The magnesium group was pretreated with 50 mg/kg MgSO4, and the other two groups received the same volume of isotonic saline. Anesthesia was induced with alfentanil, propofol, and either 0.6 mg/kg (rocuronium-0.6 and magnesium groups) or 0.9 mg/kg (rocuronium-0.9 group) rocuronium. An anesthesiologist, blinded to the group assignments, performed RSI and assessed the intubating conditions. Systolic arterial pressure (SAP) and heart rate (HR) were recorded before the magnesium sulfate or normal saline was administered, before anesthesia induction, before intubation, and every minute after intubation for 5 min. Results: Airway features were similar among the three groups. The intubating conditions were improved significantly in the magnesium group (P < 0.001) compared with the other two groups. Significant increases in SAP at 1 min after intubation were observed in the rocuronium-0.6 and -0.9 groups when compared with the magnesium group (P < 0.05). HR was comparable among the three groups (P > 0.05). No hypertensive episode occurred during the immediate post-intubation period in the magnesium group (P = 0.001), and tachycardia occurred most frequently in the rocuronium-0.6 group (P < 0.05). Conclusions: MgSO4 administered prior to RSI using alfentanil, propofol, and rocuronium may improve intubating conditions and prevent post-intubation hypertension.
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박인재,JerngChangYoon,SeongJooPark,EungHoKim,Yeon-JaeCho,Kwang-SooShin 한국미생물학회 2003 The journal of microbiology Vol.41 No.2
Four proteolytic bacteria were isolated and identified from a rotating biological contactor based on Bacillus. The four isolates, Ni 26, 36, 39 and 49 were identified as B. vallismortis, B. subtilis, Aeromonas hydrophila and B. amyloliquefaciens, respectively, based on their biochemical properties and 16S rDNA sequence analyses. The optimal proteolytic activity was observed in the temperature and pH ranges of 40-70ºC and 8.0-8.5, respectively. The proteolytic activities of all the isolates were partially inhibited by phenylmethylsulfonylfluoride (PMSF), and the isolates Ni 26, Ni 39 and Ni 49 were inhibited by the metalloprotease inhibitor, 1,10-phenanthroline. Zymographic analyses of the culture supernatants revealed the presence of at least two proteases in all isolates.
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Soo-JinCho,Jong-HoPark,SeongJooPark,Jong-SoonLim,EungHoKim,Yeon-JaeCho,Kwang-SooShin 한국미생물학회 2003 The journal of microbiology Vol.41 No.3
Extracellular protease, from Aeromonas hydrophila Ni 39, was purified 16.7-fold to electrophoretic homogeneity with an overall yield of 19.9%, through a purification procedure of acetone precipitation, and Q Sepharose and Sephacryl S-200 chromatographies. The isoelectric point of the enzyme was 6.0 and the molecular mass, as determined by Sephacryl S-200 HR chromatography, was found to be about 102 kDa. SDS/PAGE revealed that the enzyme consisted of two subunits, with molecular masses of 65.9 kDa. Under standard assay conditions, the apparent Km value of the enzyme toward casein was 0.32 mg/ml. About 90% of the proteolytic activity remained after heating at 60oC for 30 min. The highest rate of azocasein hydrolysis for the enzyme was reached at 60oC, and the optimum pH of the enzyme was 9.0. The enzyme was inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), by about 87.9%, but not by E64, EDTA, pepstatin or 1,10-phenanthroline. The enzyme activity was inhibited slightly by Ca2+, Mg2+ and Zn2+ ions.
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