Ginsenosides Enhance the Transduction of Tat-Superoxide Dismutase into Mammalian Cells and Skin

최수영,김대원,음원식,장상호,Chang Sik Yoon,최희순,Soo Hyun Choi,Young Hoon Kim,So Young Kim,Eun Shil Lee,Nam-In Baek,Hyeok Yil Kwon,Jin Hi Choi,Yoon Chul Choi,Oh-Shin Kwon,조성우,Kyuhyung Han,Kil Soo Lee,Jinseu Park 한국분자세포생물학회 2003 Molecules and cells Vol.16 No.3

Human Liver Catalase: Cloning, Expression and Characterization of Monoclonal Antibodies

최수영,Li Hua Jin,김대원,음원식,Chang Sik Yoon,장상호,최희순,Soo Hyun Choi,Young Hoon Kim,So Young Kim,Mi Ryoung Jung,강태천,원무호,Hyeon Yong Lee,Jung Hoon Kang,Oh-Shin Kwon,조성우,Kil Soo Lee,Jinseu Park 한국분자세포생물학회 2003 Molecules and cells Vol.15 No.3

GABA transaminase 의 새로운 보조인자 유사체로서의 6 - Br - pyridoxal - 5 - phosphate

최수영,위세찬,김두식 ( Soo Young Choi,Sechan Wee,Doo Sik Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2

6-Br-pyridoxal-5-phosphate, a new cofactor analog of pyridoxal-5-phosphate, was synthesized and purified homogeneously by organic and enzymatic methods. This cofactor analog binds to cofactor binding site of GABA transaminase. Resolved and reduced GABA transaminase restore the catalytic activity by 6-Br-PLP. These results indicate that the 6-Br-PLP remains covalently attached to the amino acid residue of the catalytic site and acts like natural cofactor.

4 - Aminobutyrate aminotransferase 의 촉매기능과 구조적 특성

최수영,김두식 ( Soo Young Choi,Doo Sik Kim ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.5

4-Aminobutyrate aminotransferase (GABA transaminase) was inactivated by either lysyl or sulfhydryl reagents. The inhibitory effect was protected by α-ketoglutarate, one of the substrate of GABA transaminase. These are powerful evidence that lysyl and cysteinyl residues are located in catalytic domain of the enzyme. The function of the second catalytic site of the enzyme was also examined. After reduction with NaBH₄followed by cofactor reconstitution, the reduced enzyme was capable of catalyzing transamination reaction of the amino substrate, such as 4-aminobutyrate, β-alanine or 5-aminovalerate. Since there is no significant difference in the catalytic parameter between the native and reduced enzymes, it seems reasonable to conclude that the additional catalytic site is functionally identical to the catalytic site of the native enzyme. Moreover, apoenzyme undergoes conformational changes upon binding of cofactor pyridoxal-5-phosphate (PLP) which indicates that apoenzyme becomes conformationally stabilized as a consequence of the cofactor binding.

RF 마그네트론 스퍼터링법으로 증착된 CdS 박막의 CdCl₂ 열처리 효과

최수영,천승주,정영훈,이승훈,배수현,탁성주,김지현,김동환,Choi, Su-Young,Chun, Seung-Ju,Jung, Young-Hun,Lee, Seung-Hun,Bae, Soo-Hyun,Tark, Sung-Ju,Kim, Ji-Hyun,Kim, Dong-Hwan 한국재료학회 2011 한국재료학회지 Vol.21 No.9

The CdS thin film used as a window layer in the CdTe thin film solar cell transports photo-generated electrons to the front contact and forms a p-n junction with the CdTe layer. This is why the electrical, optical, and surface properties of the CdS thin film influence the efficiency of the CdTe thin film solar cell. When CdTe thin film solar cells are fabricated, a heat treatment is done to improve the qualities of the CdS thin films. Of the many types of heat treatments, the $CdCl_2$ heat treatment is most widely used because the grain size in CdS thin films increases and interdiffusion between the CdS and the CdTe layer is prevented by the heat treatment. To investigate the changes in the electrical, optical, and surface properties and the crystallinity of the CdS thin films due to heat treatment, CdS thin films were deposited on FTO/glass substrates by the rf magnetron sputtering technique, and then a $CdCl_2$ heat treatment was carried out. After the $CdCl_2$ heat treatment, the clustershaped grains in the CdS thin film increased in size and their boundaries became faint. XRD results show that the crystallinity improved and the crystalline size increased from 15 to 42 nm. The resistivity of the CdS single layer decreased from 3.87 to 0.26 ${\Omega}cm$, and the transmittance in the visible region increased from 64% to 74%.

6-Br-Pyridoxal-5-Phosphate a New Cofactor Analog of GABA Transaminase

최수영,위세찬,김두식,Choi, Soo-Young,Wee, Se-Chan,Kim, Doo-Sik 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2

여러 효소의 자연적인 보조인자인 pyridoxal-5-phosphate의 새로운 유사체로서 6-Br-pyridoxal-5-phosphate를 유기합성과 효소를 이용한 합성방법에 의해 순수분리 정제하였다. 자외선 흡수 또는 형광 분광법에 의해 이 보조인자 유사체는 신경조직에서 신경전달물질의 하나로 알려진 GABA (4-aminobutyate)의 분해효소인 GABA transaminase의 보조인자 결합자리에 붙어서 resolved 또는 reduced GABA transaminase의 효소 활성도를 복구시켰다. 이러한 사실들은 6-Br-PLP가 GABA transaminase의 catalytic site에 있는 아미노산과 공유결합을 하여 자연적인 보조인자와 같은 역할을 한다고 볼 수 있다. 6-Br-pyridoxal-5-phosphate, a new cofactor analog of pyridoxal-5-phosphate, was synthesized and purified homogeneously by organic and enzymatic methods. This cofactor analog binds to cofactor binding site of GABA transaminase. Resolved and reduced GABA transaminase restore the catalytic activity by 6-Br-PLP. These results indicate that the 6-Br-PLP remains covalently attached to the amino acid residue of the catalytic site and acts like natural cofactor.

Tat-mediated Protein Transduction of Human Brain Pyridoxine-5-POxidase into PC12 Cells

최수영,박진서,이선화,이길수,음원식,조성우,원무호,권오신,강태천,Seok-Il Hwang,Soo Hyun Choi,김대원,Jae Jin An,So Young Kim 한국생화학분자생물학회 2006 BMB Reports Vol.39 No.1

Pyridoxine-5-P oxidase catalyses the terminal step in thebiosynthesis of pyridoxal-5-P, the biologically active formof vitamin B6 Which acts as an essential cofactor. Here, ahuman brain pyridoxine-5-P oxidase gene was fused with agene fragment encoding the HIV-1 Tat protein transductiondomain (RKKRRQRRR) in a bacterial expression vectorto produce a genetic in-frame Tat-pyridoxine-5-P oxidasefusion protein. Expressed and purified Tat-pyridoxine-5-Poxidase fusion protein transduced efficiently into PC12cells in a time- and dose-dependent manner when addedexogenously to culture media. Once inside the cells, thetransduced Tat-pyridoxine-5-P oxidase protein showedcatalytic activity and was stable for 48 h. Moreover, theformation of pyridoxal-5-P was increased by adding exogenousTat-pyridoxine-5-P oxidase to media pre-treated with thevitamin B6 precursor pyridoxine. In addition, the intracellularconcentration of pyridoxal-5-P was markedly increasedwhen Tat-pyridoxal kinase was transduced together withTat-pyridoxine-5-P oxidase into cells. These results suggestthat the transduction of Tat-pyridoxine-5-P oxidase fusionprotein presents a means of regulating the level ofpyridoxal-5-P and of replenishing this enzyme in variousneurological disorders related to vitamin B6.

이온빔 보조 증착법에 의한 TiN 박막도포가 니켈-크롬-베릴륨 합금의 표면 성상에 미치는 영향에 관한 연구

최수영,이선형,장익태,양재호,정헌영,Choi, Soo-Young,Lee, Sun-Hyung,Chang, Ik-Tae,Yang, Jae-Ho,Chung, Hun-Young 대한치과보철학회 1999 대한치과보철학회지 Vol.37 No.2

Dental restorative materials must have the physical properties to withstand wear and corrosion. Base metal alloys possess better mechanical properties and lower price than the gold alloys. For these reasons such alloys have largely replaced the precious metal alloys. One aspect to con-sider is the release of metal substances to oral environment. The release of elements from dental alloys is a continuing concern because the elements may have the potentially harmful biological effects on local tissues. The purpose of this study was to minimize metal release on the nonprecious metal surfaces by ion beam assisted deposition(IBAD) of titanium nitride (TiN) Ni-Cr-Be alloys with and without TiN coatings were secured in an wear test machine opposing ruby ball to determine their relative resistance to wear with loom, 200m, 300m and 400m sliding distance. And the corrosion behavior of the Ni-Cr-Be alloys with and without TiN coatings and 3 dental noble alloys have been studied. Potentiodynamic curves were used to analyse the corrosion characteristics of the alloys. The measurement of the released Ni and Cr ions was conducted by analysis of the electrolyte solution with atomic absorption spectroscopy. The results were as follows : 1. The critical sliding distance that wore down TiN coatings of $2.5{\mu}m$ thickness in this study condition was 300m. 2. Ion beam assisted deposition of TiN showed a good surface modification with respect to the properties of wear and corrosion resistance. 3. X-ray diffraction showed that the strongest peak of TiN is TiN(111) in the coatings. 4. The release of Ni and Cr ions from alloys measured by means of atomic absorption spectroscopy was reduced by ion beam assisted deposition of TiN.

단일병원 신생아 환자의 메티실린내성 황색포도알균 보균율

최수영,한상우,윤혜선,기모란,Choi, Soo Young,Han, Sang Woo,Yoon, Hye Sun,Ki, Moran 대한소아감염학회 2012 Pediatric Infection and Vaccine Vol.19 No.3

Purpose: The aim of this study is to investigate the colonization rate of Methicillin-resistant Staphylococcus aureus (MRSA) in neonates by different clinical characteristics, to presume the origin of MRSA acquisition, and to identify the risk factors associated with MRSA colonization. Methods: We retrospectively reviewed the medical records of 1,733 neonates admitted to Seoul Eulji hospital Neonatal Intensive Care Unit between January 2008 and December 2011. Nasal, inguinal and rectal swab specimens were obtained upon admission and each week until discharge. We classified the route of MRSA acquisition as; hospital associated (HA-MRSA) and community associated (CA-MRSA) according to the case definition. Results: Among 1,733 neonates, 415 (23.9%) were colonized with MRSA. Gestational age, birth weight, delivery type, maternal antibiotics usage before delivery, birth place and care place before admission were influencing factors in colonization of MRSA. The colonization rate was significantly high in neonates without maternal prophylactic antibiotics use before delivery than in the other group (relative risk 2.77, 95% CI 1.88-4.07; P<0.01), and outborns showed higher MRSA colonization rate compared to inborns (relative risk 2.28, 95% CI 1.17-4.42; P=0.015). Conclusion: We identified the neonatal MRSA colonization rate to be 23.9%. We estimated HA-MRSA colonization rate to be 10% (51/511) and CA-MRSA colonization rate to be 36% (309/858). We ascertained that risk factors in MRSA colonization in neonates were prophylactic use of antibiotics in mothers and the birth place. 목 적 : 단일 병원 신생아입원실에 입원한 신생아를 대상으로 환자의 임상적 특징에 따른 MRSA 보균율을 알아보고, 그 기원을 추정해 보며, MRSA 보균에 영향을 미치는 요소들을 살펴보고자 하였다. 방 법 : 2008년 1월부터 2011년 12월까지 을지대학교 서울 을지병원 신생아 입원실에 입원하여 MRSA 감시배양검사를 시행받은 1,733명의 신생아를 대상으로 의무기록을 후향적으로 조사하였다. MRSA 감시배양검사는 비강, 서혜부, 직장에서 시행하였고, 퇴원 시까지 매주 반복 시행 하였다. MRSA 감시배양결과에 따라서 보균자와 비보균자로 나누었다. 결 과 : 대상환자 1,733명 중에 415명(23.9%)이 MRSA 보균자였다. 제태기간, 출생체중, 분만 방식, 분만전 산모에게 항생제 투여 여부, 출생장소, 입원전 체류 장소에 따라서 MRSA 보균율에 차이를 보였다(P<0.001). 다변량 검사에서 분만전 산모에게 예방적 항생제를 투여하지 않은 경우가 투여한 경우에 비해서 신생아가 MRSA 보균자가 될 위험도가 2.8배(OR=2.77; 95% CI, 1.88-4.07), 출생장소가 외부인 경우가 본원인 경우에 비해서 2.3배(OR=2.28; 95% CI, 1.17-4.42) 높음을 확인하였다. 결 론 : 신생아 입원환자를 대상으로 한 MRSA 보균율은 23.9%로 상대적으로 높은 보균율을 확인하였다. 환자특성을 고려하여 추정한 HA-MRSA 보균율은 51/511명(10%), CA-MRSA 보균율은 309/858명(36%) 이었다. 본병원 신생아에서 MRSA 보균과 연관된 요인은 산모의 예방적 항생제 사용여부와 출생장소임을 확인하였다.

Catalytic and Structural Properties of 4-Aminobutyrate Aminotransferase

최수영,김두식,Choi, Soo-Young,Kim, Doo-Sik 생화학분자생물학회 1991 한국생화학회지 Vol.24 No.5

4-Aminobutyrate aminotransferase(GABA transaminase)는 lysyl group에 특이한 Bis-PLP나 -SH group에 특이한 DTNB 또는 DPD에 의하여 효소가 불활성화 되었으며 이 불활성화는 효소의 기질인 ${\alpha}$-ketoglutarate의 결합부위에 lysyl group과 cysteinyl group이 위치하고 있음을 보여주는 것이다. GABA transaminase의 second catalytic site에 대한 구조적 특성을 밝히기 위하여 native 효소를 $NaBH_4$로 환원시킨 후 몇 가지 아미노산 기질을 이용하여 kinetic parameters를 조사해 본 결과 큰 차이가 없음을 알 수 있었다. 이는 second catalytic site가 구조적으로나 작용기적으로 native 효소의 catalytic site와 같다는 것을 나타낸다. 마지막으로 native 효소에서 cofactor가 떨어졌을 때(apo 효소) 구조적 변화를 가져왔다. 이는 효소가 in vivo에서 합성될 때 불안정한 apo enzyme으로 만들어진 후 cofactor가 binding 함으로써 촉매 기능적으로 또는 구조적으로 안정화 된다고 본다. 4-Aminobutyrate aminotransferase (GABA transaminase) was inactivated by either lysyl or sulfhydryl reagents. The inhibitory effect was protected by ${\alpha}$-ketoglutarate, one of the substrate of GABA transaminase. These are powerful evidence that lysyl and cysteinyl residues are located in catalytic domain of the enzyme. The function of the second catalytic site of the enzyme was also examined. After reduction with $NaBH_4$ followed by cofactor reconstitution, the reduced enzyme was capable of catalyzing transamination reaction of the amino substrate, such as 4-aminobutyrate, ${\beta}$-alanine or 5-aminovalerate. Since there is no significant difference in the catalytic parameter between the native and reduced enzymes, it seems reasonable to conclude that the additional catalytic site is functionally identical to the catalytic site of the native enzyme. Moreover, apoenzyme undergoes conformational changes upon binding of cofactor pyridoxal-5-phosphate (PLP) which indicates that apoenzyme becomes conformationally stabilized as a consequence of the cofactor binding.