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Chung Un Lee,Minyong Kang,Hyun Hwan Sung,Hwang Gyun Jeon,Deok Hyun Han,Byung Chang Jeong,Seong Soo Jeon,Hyun Moo Lee,Han Yong Choi,Seong Il Seo 대한비뇨기종양학회 2017 대한비뇨기종양학회지 Vol.15 No.3
Purpose: To compare the 5-year oncologic and functional outcomes of robot-assisted laparoscopic partial nephrectomy (RALPN) and laparoscopic partial nephrectomy (LPN) as treatment for localized renal cell carcinoma (RCC). Materials and Methods: We analyzed the records of 181 patients with localized RCC who underwent RALPN (n=97) or LPN (n=84) between 2007 and 2011. Demographic and preoperative data with estimated glomerular filtration rate (eGFR), intraoperative data including warm ischemic time (WIT) and complications, oncologic outcomes (recurrence, metastasis), and rate of eGFR preservation at most recent follow-up were examined. Results: WIT was shorter in the RALPN group (27±9.1 minutes) than the LPN group (31±10 minutes, p=0.019). Intraoperative complication rates were also lower in RALPN patients than LPN patients (4.1% vs. 14.3%). The eGFR preservation rate was higher in the RALPN group (84.6%) than in the LPN group (81.5%, p=0.049). Particularly, a relatively high difference in the eGFR preservation rate was observed in the RALPN group compared with the LPN group according to R.E.N.A.L. score 7–10 values (RALPN, 86.5±12.9 vs. LPN, 76.7±16.0; p=0.003). During the follow-up period, there was no local recurrence in either group and distant metastases only occurred in one patient in the RALPN group and in 2 patients in the LPN group. Conclusions: RALPN and LPN showed similar 5-year oncologic outcomes, but RALPN was superior to LPN in terms of WIT, intraoperative complications, and long-term eGFR preservation rate, especially in complex cases.
Chung Tae-Wook,Lee Dong-Ick,Kim Dong-Soo,Jin Un-Ho,Park Chun,Kim Jong-Guk,Kim Min-Gon,Ha Sang-Do,Kim Keun-Sung,Lee Kyu-Ho,Kim Kwang-Yup,Chung Duck-Hwa,Kim Cheorl-Ho The Microbiological Society of Korea 2006 The journal of microbiology Vol.44 No.3
Two pathways of ammonium assimilation and glutamate biosynthesis have been identified in microorganisms. One pathway involves the NADP-linked glutamate dehydrogenase, which catalyzes the amination of 2-oxoglutarate to form glutamate. An alternative pathway involves the combined activities of glutamine synthetase, which aminates glutamate to form glutamine, and glutamate synthase, which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. We have cloned the large subunit of the glutamate synthase (GOGAT) from Salmonella typhimurium by screening the expression of GOGAT and complementing the gene in E. coli GOGAT large subunit-deficient mutants. Three positive clones (named pUC19C12, pUC19C13 and pUC19C15) contained identical Sau3AI fragments, as determined by restriction mapping and Southern hybridization, and expressed GOGAT efficiently and constitutively using its own promoter in the heterologous host. The coding region expressed in Escherichia coli was about 170 kDa on SDS-PAGE. This gene spans 4,732 bases, contains an open reading frame of 4,458 nucleotides, and encodes a mature protein of 1,486 amino acid residues (Mr =166,208). The EMN-binding domain of GOGAT contains 12 glycine residues, and the 3Fe-4S cluster has 3 cysteine residues. The comparison of the translated amino acid sequence of the Salmonella GOGAT with sequences from other bacteria such as Escherichia coli, Salmonella enterica, Shigella flexneri, Yersinia pestis, Vibrio vulnificus and Pseudomonas aeruginosa shows sequence identity between 87 and 95%.