전통적 운동 심상 패러다임을 통해 육상트랙을 반시계방향으로 뛸 때의 특정적 뇌 활성화: fMRI 연구

권세창(Sechang Kwon),김진구(Jingu Kim),김유진(Yujin Kim) 한국여성체육학회 2021 한국여성체육학회지 Vol.35 No.2

심상으로 운동장을 반시계 방향으로 돌 때의 정서변화: 대뇌반구의 비대칭적 활성화에 관한 탐색적 연구

권세창 ( Kwon Sechang ),김진구 ( Kim Jingu ),김유진 ( Kim Yujin ) 한국체육학회 2020 한국체육학회지 Vol.59 No.3

본 연구의 목적은 왜 사람들이 운동장을 반시계방향으로 도는가에 대한 궁금증을 풀기 위한 예비연구이다. 참가자들이 시계 및 반시계방향으로 운동심상을 할 때 정서와 EEG 대뇌반구 비대칭의 차이지표를 분석하여 방향에 따른 심리적 변화를 알아보았다. 피험자는 평균나이는 20.5세의 대학생으로 총 20명(남자 10명, 여자 10명)을 대상으로 하였고, 피험자를 무작위로 두 그룹인 시계방향(CW)과 반시계방향(CCW)으로 나누어 실험을 진행하였다. 실험과제는 1인칭 시점의 운동심상 과제로 모든 피험자에게 1800ms 동안 화면에 나타나는 육상트랙의 곡선구간을 달리는 심상을 하도록 지시하였다. 뇌파의 주요 측정영역은 전전두영역(Fp1, Fp2), 전두영역(F3, F4), 중앙영역(C3, C4)이었고, 자료 분석은 측정영역의 알파파에 대한 집단 간 독립표본 t검정을 실시하였다. 본 연구결과로 전두엽에서 집단 간 유의한 비대칭 차이가 있는 것으로 나타났다. 특히, CW 그룹에서는 좌반구(F3)에 비해 우반구(F4)의 활동이 높은 것으로 나타났고, CCW 그룹에서는 우반구보다 좌반구의 활동이 상대적으로 높은 것으로 나타났다. 이와 같은 결과는 운동장을 시계방향으로 달릴 때는 부정적 정서가 그리고 반시계방향으로 달릴 때는 긍정적 정서가 나타날 수 있음을 의미한다. 이 연구는 운동 수행에 있어 방향성에 따라 정서적 변화가 다르게 나타날 수 있고, 이러한 정서적 변화들로 인해 방향편향이 결정되어질 수 있음을 신경생리학적으로 알아본 것에 그 의미가 있다. The purpose of this study was to investigate affective changes through EEG asymmetry when subjects run around each curved track, counterclockwise (CCW) and clockwise (CW). A total of 20 (10 females and 10 males; M age=20.5) subjects, all of whom were right-handed, participated in the study. According to different directional conditions, all subjects were randomly divided into two groups which were CCW and CW, and the gender ratio was definitely considered as the same. Using the motor imagery (MI) task, they were instructed to start MI when presented with a dynamic image showing the first person view of running a curved track in either direction for 1800ms. The frontal (Fp2-Fp1, F4-F3) and central (C4-C3) lobes of each subject were measured while they were performing MI. The independent t-test was conducted to determined differences in the alpha values between directional conditions. As a result, there was a significant difference in the frontal lobe (F4-F3) between conditions. Especially, subjects in the CW condition displayed greater right frontal activity (F4), while greater l eft f rontal activity (F3) was observed in the CCW condition. It means that running around a t rack counterclockwise is predictive of greater left frontal activity which indicates more positive affect while running around a track clockwise is expected to be greater right frontal activity which can be interpreted in association with negative affect. In conclusion, the result of this study demonstrated that affective changes can be appear depending on different directional conditions and then be closely associated to the formation of turning bias.

운동 심상을 이용한 결과지식 지연간격에 따른 대뇌 감각운동영역의 활성화에 대한 탐색적 연구

권세창(Kwon, Se-Chang) 한국코칭능력개발원 2022 코칭능력개발지 Vol.24 No.5

피브로인 미세구 첨가에 의한 3T3 섬유아 세포의 이동 촉진

권세창(Se Chang Kwon),전현상(Hyun Sang Jeon),류다영(Da Yeong Ryu),김지영(Ji Young Kim),허원(Won Hur) 한국생물공학회 2018 KSBB Journal Vol.33 No.1

Microsphere-stimulated cell migration was observed at the periphery of a confluent 3T3 cell culture even in the absence of serum. Under non-contact inhibition conditions, 3T3 cells showed a highest migratory velocity of 1.7 μm/min in a DMEM media with 0.05 mg/mL microspheres. It is 147% faster than those in DMEM with 10% serum and 194% faster than those in DMEM only. Monolayer colonies were formed from 3T3 cell spheroids in a microsphere-containing culture medium but not in a DMEM without serum. Western blot analysis showed that microsphere supplementation reduced the expression levels of focal adhesion kinase. Fibroin microsphere seems to stimulate a migratory signal cue other than focal adhesion kinase. Unlike to other nanoparticles, fibroin microspheres stimulated 3T3 cell migration, showing a potential candidate for wound healing stimulation.

Xanthomonas holcicola 에서 Xhaoll endonuclease 분리 및 성질

권세창,조진만,강정훈,조영동 ( Se Chang Kwon,Jin Man Cho,Jung Hoon Kang,Joo Hoon Kim,Young Dong Cho ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.2

XhoII endonuclease was purified from Xanthomonas holcicola by streptomycin sulfate fractionation, phosphocellulose, heparin agarose, Sephadex G-100, DNA-cellulose and DEAE-sephacel column chromatography. The molecular weight of XhoII endonuclease was 76,000 measured by Sephadex G-100 and G-200 column chromatography. 22,000 units of XhoII endonuclease was obtained from 100 g of cell paste. XhoII endonuclease has an optimum temperature of 37℃ with pH 7.5 to 8.0. XhoII endonuclease activity was remarkably inhibited above a NaCI concentration of 150 mM. XhoII endonuclease activity was also severely inhibited above 0.5 mM NEM and 1 mM DTNB, the thiol group modification reagents, and 3 mM phenylglyoxal, the arginine modification reagent. But XhoII endonuclease from inactivation by these reagents was protected by substrate DNA. So there is a possibility that the thiol group and arginine residue play an important role in the XhoII endonuclease activity.

제한 효소 EcoRl 의 활성에 관여하는 Serine 잔기 및 그 위치에 관한 연구

권세창,조영동 ( Se Chang Kwon,Young Dong Cho ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2

EcoRl endonuclease is inactivated by diisopropylfluorophosphate (DFP), a serine residue modification reagent. The rate of inactivation is reduced by the substrate DNA and Mg^(++), The DNA cleavage activity of EcoRI endonuclease in inactivated by DFP, while the binding capacity of enzyme is not inactivated. Several lines of experimental evidence indicate that serine residue plays a very important catalytic role is EcoRI endonuclease. To generate peptide maps of the active serine residue region, the enzyme was labeled with (³H)DFP and digested with trypsin. The amino acid composition of the labeled peptide corresponds to a tryptic fragment including residues 146-169 in the EcoRI endonuclease sequence.

The Role of Histidyl Residues in EcoRI Endonuclease

권세창,조진만,조영동,Kwon, Se-Chang,Cho, Jin-Man,Cho, Young-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.3

제한효소 Eco RI을 histidine residue에 반응하는 diethylpyrocarbonate(DEP)와 반응시킨 결과 효소 활성이 감소함을 알 수 있었다. 효소 활성이 90% 정도 감소할 때까지 반응은 pseudo-first order kinetics를 따랐고 DEP와 더 반응시키면 효소 활성이 완전히 없어졌다. DEP에 의한 효소의 비활성화는 기질인 pUC9 DNA에 의해 보호됨을 알 수 있었고 1개의 histidine residue가 효소 활성에 관여하는 것으로 나타났다. 그리고 DEP에 의해 비활성화된 효소에 과량의 hydroxylamine을 첨가하여 주면 재활성이 나타났다. 한편 histidine residue의 역할을 알아보고자 DEP가 제한효소 EcoRI의 기질 결합 능력에 미치는 영향을 조사하였다. 효소의 기질 결합 능력도 DEP 농도를 증가시킴에 따라 감소하였고 기질에 대한 보호 효과와 hydroxylamine에 의한 재활성화가 위의 효소 비활성화와 비슷하게 나타났다. 따라서 제한효소 EcoRI의 비활성화는 기질에 결함을 하지 못함으로써 나타난 것으로 생각된다. 이런 결과에 따르면 제한 효소 EcoRI의 활성에 histidine residue가 관여하며 이 residue는 기질에 대한 결합 기작에 관여하는 것으로 사료된다. Treatment of EcoRI endonuclease with the histidine modification reagent, diethylpyrocarbonate(DEP), resulted in enzyme inactivation. The reaction followed pseudo first-order kinetics until 90 to 95% of the enzyme had been inactivated. And prolonged incubation with DEP resulted in complete inactivation. When the modification reaction was carried out after preincubation with pUC9 DNA as substrate, the rate of inactivation was significantly decreased. The kinetics of inactivation indicate that the reaction of 1 molecule of DEP reagent is necessary for inactivation of each active site in EcoRI endonuclease. The inactivation of EcoRI endonuclease by DEP was partially reversed upon addition of excess hydroxy lamine. The effects of DEP on the binding ability of EcoRI endonuclease to its substrate, pUC9 DNA, were also investigated. When EcoRI endonuclease was preincubated with substrate DNA, the binding capacity was recovered significantly which suggests protection of the binding activity from DEP. Binding activity was also recovered with addition of hydroxylamine. The inhibition of activity, protection by DNA from DEP modification or reactivation by addition of hydroxylamine show similar tendencies to that of catalytic and binding properties. The cumulative results suggest that histidine residue plays a very important role as a binding residue in EcoRI endonuclease.

Purification and Characterization of XhoII Endonuclease from Xanthomonas holcicola

권세창,조진만,강정훈,김주훈,조영동,Kwon, Se-Chang,Cho, Jin-Man,Kang, Jung-Hoon,Kim, Joo-Hoon,Cho, Young-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.2

XhoII endonuclease를 Xanthomonas holcicola로부터 분리 하였으며 여러 group specific reagents를 사용하여 효소의 비활성화, 기질에 의한 비활성화 억제와 비활성화된 효소의 재활성화 등을 조사하여 효소 활성에 관여하는 amino acid residue를 조사하였다. XhoII endonuclease의 분자량은 gel filteration을 통해 76,000으로 나타났고 이 효소의 최적온도는 $37^{\circ}C$이고 pH7.5에서 8.0사이에는 활성도에 변화을 주지 않는 최적 pH임이 밝혀졌다. XhoII endonuclease에 group specific reagents인 phenylglyoxal(arginine), PLP와 O-phthalaldehyde(lysine), DTNB와 NEM(cysteine) 그리고 DFP (serine)을 적용시킨 결과 효소활성이 억제되었다. DTNB와 NEM, phenylglyoxal 그리고 DFP에 의한 효소활성 억제에 대한 기질인 pUC9 DNA가 보호 효과를 보였으며 특히 DTNB와 NEM에 의한 효소의 비활성화는 ${\beta}$-MSH에 의해 활성이 회 복되었다. 이런 결과로 XhoII endonuclease활성에 arginne, serine 그리고 cysteine residue가 관여할 것이라 생각되며 특히 cysteine residue가 중요한 역할을 하고 있을 것이라 사료된다. XhoII endonuclease was purified from Xanthomonas holcicola by streptomycin sulfate fractionation, phosphocellulose, heparin agarose, Sephadex G-100, DNA-cellulose and DEAE-sephacel column chromatography. The molecular weight of XhoII endonuclease was 76,000 measured by Sephadex G-100 and G-200 column chromatography. 22,000 units of XhoII endonuclease was obtained from 100 g of cell paste. XhoII endonuclease has an optimum temperature of $37^{\circ}C$ with pH 7.5 to 8.0. XhoII endonuclease activity was remarkably inhibited above a NaCl concentration of 150 mM. XhoII endonuclease activity was also severely inhibited above 0.5 mM NEM and 1 mM DTNB, the thiol group modification reagents, and 3 mM phenylglyoxal, the arginine modification reagent. But XhoII endonuclease from inactivation by these reagents was protected by substrate DNA. So there is a possibility that the thiol group and arginine residue play an important role in the XhoII endonuclease activity.

Evidence that Serine Residue is Essential for Enzyme Activity and Identification of $(^3H)$ Diisopropylfluorophosphate labeled Peptide in EcoRI Endonuclease

권세창,조영동,Kwon, Se-Chang,Cho, Young-Dong 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2

제한 효소 EcoRI은 serine 잔기에 특이적으로 결합하는 diisopropylfluorophosphate (DFP)에 의해 비활성화 되었다. 이러한 비활성화 속도는 $Mg^{++}$과 기질인 DNA에 의해서 감소하였다. DFP의 작용은 제한 효소 EcoRI의 DNA 절단 활성에 영향을 주는 반면에 DNA 결합 활성에는 영향을 주지 않는 것으로 나타났다. 이러한 결과들로부터 제한 효소 EcoRI에서 serine 잔기가 절단 활성에 관여하고 있을 것으로 사료된다. 효소 활성에 관여하는 serine 잔기의 위치를 확인하기 위하여 $[_3H]$-DFP를 사용한 결과 제한 효소 EcoRI의 146-169 사이에 존재하는 serine 잔기임을 알 수 있었다. EcoRI endonuclease is inactivated by diisopropylfluorophosphate (DFP), a serine residue modification reagent. The rate of inactivation is reduced by the substrate DNA and $Mg^{++}$. The DNA cleavage activity of EcoRI endonuclease in inactivated by DFP, while the binding capacity of enzyme is not inactivated. Several lines of experimental evidence indicate that serine residue plays a very important catalytic role is EcoRI endonuclease. To generate peptide maps of the active serine residue region, the enzyme was labeled with $(^3H)$DFP and digested with trypsin. The amino acid composition of the labeled peptide corresponds to a tryptic fragment including residues 146-169 in the EcoRI endonuclease sequence.

제한효소 Eco Rl의 Histidine Residue 역할에 관한 연구

권세창,조진만,조영동 ( Se Chang Kwon,Jin Man Cho,Young Dong Cho ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.3

Treatment of EcoRI endonuclease with the histidine modification reagent, diethylpyrocarbonate(DEP), resulted in enzyme inactivation. The reaction followed pseudo first order kinetics until 90 to 95% of the enzyme had been inactivated. And prolonged incubation with DEP resulted in complete inactivation. When the modification reaction was carried out after preincubation with pUC9 DNA as substrate, the rate of inactivation was significantly decreased. The kinetics of inactivation indicate that the reaction of 1 molecule of DEP reagent is necessary for inactivation of each active site in EcoRI endonuclease. The inactivation of EcoRl endonuclease by DEP was partially reversed upon addition of excess hydroxylamine. The effects of DEP on the binding ability of EcoRI endonuclease to its substrate, pUC9 DNA, were also investigated. When EcoRI endonuclease was preincubated with substrate DNA, the binding capacity was recovered significantly which suggests protection of the binding activity from DEP. Binding activity was also recovered with addition of hydroxylamine. The inhibition of activity, protection by DNA from DEP modification or reactivation by addition of hydroxylamine show similar tendencies to that of catalytic and binding properties. The cumulative results suggest that histidine residue plays a very important role as a binding residue in EcoRI endonuclease.