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공복시 당뇨 환자와 일반인에서 모세혈 혈당 측정의 정확도: ISO 15197:2013 지침에 따른 G300의 성능 평가
지영민,서민희,유병욱,홍성호,조주연,조용진,오정은,신경숙 대한임상건강증진학회 2017 Korean Journal of Health Promotion Vol.17 No.4
Background:Self-monitoring of blood glucose plays an important role in management of diabetes mellitus. Blood glucose measurement is based on using plasma glucose separated from whole blood, but many people with diabetes and health care providers use a portable glucose meter for convenience. The aim of this study was to evaluate the accuracy and agreement of G300 portable glucose monitoring system against standard venous glucose testing methods, based on ISO 15197:2013 standards. Methods:This study was the evaluation of G300 system accuracy following ISO 15197:2013 standards. We estimated precision, system accuracy, hematocrit interference, interfering substances, and user performance. Results:In repeatability precision evaluation of those glucometers, standard deviation was 2.9-3.7 mg/dL at glucose levels under 100 mg/dL and coefficient of variation was 1.7-3.2% at glucose levels over 100 mg/dL, respectively. In accuracy evaluation, 99.5% of difference values between results of G300 portable glucose monitoring system and clinical laboratory were within 95%. Consensus Error grid analysis showed that all values (100%) are within zone A. Hematocrit range between 20% and 60% did not cause interference. These results were acceptable for the ISO15197:2013 criteria in all glucose concentrations. Conclusions:This study showed that G300 can provide reliable blood glucose results for patients and health care providers to manage diabetes mellitus, satisfying the ISO 15197:2013 criteria. 연구배경: 일반적으로 혈당의 측정은 전혈을 혈장으로 분리하여 측정하는 것을 기준으로 하고 있으나 간편하고 빠르게 측정하기 위해 자가 혈당 측정기가 환자의 가정, 외래, 병실 등에서 폭넓게 사용되고 있다. 하지만 자가 혈당측정기는 전혈을 사용하고, 검사 방법이 중앙검사실과 다르기 때문에 수행능을 평가하고, 이를 명시하여 사용자가혼란을 일으키지 않도록 하는 것이 중요하다. 이에 본 연구자들은 최근 국내에 소개되어 사용 중인 G300 혈당 측정시스템의 성능을 분석 평가하여 그 유용성을 검토하고자 한다. 방법: 본 연구는 ISO 15197 지침에 따라 G300을 사용하여 진행되었다. 채혈실에서 정맥혈을 채혈한 성인 환자 및일반인 100명을 대상으로 공복 모세혈 혈당과 정맥혈 혈당을 측정하였다. 손가락에서 측정한 모세혈은 즉시 G300 기계로 측정되었고, 정맥혈은 중앙 검사실에서 측정되었으며, 정밀도, 정확도에 대한 평가를 시행하였다. 결과: 정밀도 반복성 평가에서 100 mg/dL 미만 구간에서표준편차는 2.9-3.7 mg/dL로 5 mg/dL 미만이었고, 100 mg/dL 이상 구간에서 변이계수는 1.7-3.2% 사이에 있어5% 미만으로 우수하였다. 정확도 평가는 99.5%로 ISO 15197 기준인 95% 이상을 충족하였다. Error grid 분석 결과에서 모든 측정치는 zone A에 분포하여 기준을 충족하였다. 20%에서 60% 사이 범위의 헤마토크릿은 간섭영향을 미치지 않았고, 간섭물질 평가상 5개의 물질이 기준을초과하여 용량-반응 평가를 시행하였다. 모든 결과는 ISO 15197:2013의 지침을 만족하였다. 결론: 본 연구에서 G300은 ISO 15197 지침을 만족하는신뢰할 만한 결과를 보였으며, G300이 혈당에 대해 정확하고 신뢰할 만한 결과를 제공할 것으로 기대된다.
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Immobilization of $\alpha$-Amylase and Glucoamylase on Porous Cellulose Beads
지영민,전문진,엠써네쓰,Chi, Y.M.,Chun, M.,Sernetz, M. 생화학분자생물학회 1984 한국생화학회지 Vol.17 No.1
다공성 섬유소 업자를 제조하고, $\alpha$-amylase와 glucoamylase를 각각 효과적으로 고정화 시키기 위하여 섬유소 담체를 활성화 시키고 그 최적 조건을 조사하였으며 그것의 효소학적 성질에 관하여 연구하였다. 가장 효과적 인 $\alpha$-amylase와 glucoamylase의 고정화는 다공성 섬유소 담체를 0.1M p-benzoquinone으로 활성화 시킨 후 3% gallotannin으로 재활성화 시켰을 때 잔여 활성도가 가장 높았으며 이때 $CaCl_2$를 첨가함으로써 고정화율이 증가되었다. 유리의 $\alpha$-amylase와 고정화 $\alpha$-amylase의 반응 최적 pH는 차이가 없었으며, 반응 최적 온도는 모두 $55^{\circ}C$이었다. 유리의 glucoamylase와 고정화 glucoamylase의 반응 최적 pH에도 차이가 없었으나 반응 최적 온도는 유리의 glucoamylase는 $55^{\circ}C$, 고정화 glucoamylase는 $50^{\circ}C$로 나타났다. Starch에 대한 $\alpha$-amylase와 gucoamylase의 Km 값은 고정화시킴으로써 증가되었고 저장성 또한 증가되었다. For the immobilization of $\alpha$-amylase and glucoamylase effectively on porous cellulose beads, the optimal activation methods were studied. And their enzymatic properties were investigated. The results obtained were as follows; 1) The most effective method of enzyme immobilization was obtained when the 3% gallotannin, pH 4, was used as activation reagent after 0.1M p-benzoquinone. pH 12, activation in case of $\alpha$-amylase and when the 3% gallotannin, pH 9, was used as activation reagent after 0.1M p-benzoquinone, pH 12, activation in case of glucoamylase. 2) The immobilized enzymes activities were increased by the addition of $CaCl_2$ to immobilizing mixture. The immobilized $\alpha$-amylase activity was increased from 69.17u/g to 77.18u/g by addition of $5{\times}10^{-4}M$ $CaCl_2$ to the immobilizing mixture. The immobilized glucoamylase activity was increased from 157.37u/g to 189.31u/g by addition of $5{\times}10^{-3}M$ $CaCl_2$ to the immobilizing mixture. The maximum immobilization rate of $\alpha$-amylase was 5.07% and glucoamylase was 47.33%. 3) The optimum pH of $\alpha$-amylase was 4.5-5 for native enzyme and also 4. 5-5 for immobilized enzyme. The optimum pH of glucoamylase was 4.5 in both cases. 4) The optimum temperatures for the native and immobilized $\alpha$-amylase were both $55^{\circ}C$. The optimum temperature was $55^{\circ}C$ for the native glucoamylase and $50^{\circ}C$ for the immobilized glucoamylase. 5) The Km value of native $\alpha$-amylase was 0.48% and that of immobilized $\alpha$-amylase was 1.43% while Vmax (1.52mg hydrolyzed soluble starch/min) was unaltered. The Km value of native glucoamylase was 0.83% and that of immobilized glucoamylase was 2.0%.
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다공성 섬유소 입자에 대한 α - Amylase 와 Glucoamylase 의 고정화
지영민,전문진,엠써네쓰 ( Y . M . Chi,M . Chun,M . Sernetz ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.1
For the immobilization of α-amylase and glucoamylase effectively on porous cellulose beads, the optimal activation methods were studied. And their enzymatic properties were investigated. The results obtained were as follows; 1) The most effective method of enzyme immobilization was obtained when the 3% gallotannin, pH 4, was used as activation reagent after 0.1M p-benzoquinone, pH 12, activation in case of α-amylase and when the 3% gallotannin, pH 9, was used as activation reagent after 0.1M p-benzoquinone, pH 12, activation in case of glucoamylase. 2) The immobilized enzymes activities were increased by the addition of CaCl₂ to immobilizing mixture. The immobilized a-amylase activity was increased from 69.17 μ/g to 77.18μ/g by addition of 5×10^(-4)M CaCl₂ to the immobilizing mixture. The immobilized glucoamylase activity was increased from 157.37μ/g to 189. 31μ/g by addition of 5×10^(-3)M CaCl₂ to the immobilizing mixture. The maximum immobilization rate of a-amylase was 5.07 and glucoamylase was 47.33%. 3) The optimum pH of α-amylase was 4.5-5 for native enzyme and also 4.5-5 for immobilized enzyme. The optimum pH of glucoamylase was 4.5 in both cases. 4) The optimum temperatures for the native and immobilized α-amylase were both 55℃. The optimum temperature was 55℃ for the native glucoamylase and 50℃ for the immobilized glucoamylase. 5) The Km value of native a-amylase was 0.48% and that of immobilized α-amylase was 1.43% while Vmax (1.52㎎ hydrolyzed soluble starch/min) was unaltered. The Km value of native glucoamylase was 0.83% and that of immobilized glucoamylase was 2.0%.
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대용량 분산 클러스터 기반의 시계열 빅-데이터 처리 및 수집 시스템
지영민,유준재,서희 한국정보통신설비학회 2016 한국정보통신설비학회 학술대회 Vol.2016 No.09
The technology of IoT which began in the sensor networks generate numerous sensing data from a variety of physical environments to virtual world. There are many types of IoT device used the sensors based on application. They usually create time series data that people can use to make more sensible decision. Things produced various data which is generated and stored as time based and then saved them to the existing database. In this paper, we introduce the system architecture for the large distributed cluster based system for the processing and collecting of big-data of time-series to meet the goal of performance using Redis Cluster and OpenTSDB.
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