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Jaffe법과 효소법으로 측정한 Roche Modular D, Cobas 8000 c702 및 Beckman Coulter AU5800 장비 간의 혈청 Creatinine 비교
오종원,박형두 대한진단검사의학회 2020 Laboratory Medicine Online Vol.10 No.1
Background: Creatinine (Cr) is a representative biomarker reflecting renal function. In this study, we compared serum Cr levels using Roche Modular D (Roche Diagnostics, Germany), Roche Cobas 8000 c702 (Roche Diagnostics), and AU5800 (Beckman Coulter, USA). In addition, we assessed the differences in Cr measurements using the Jaffe and enzymatic methods. Methods: Precision, linearity, and methods were evaluated in accordance with CLSI guidelines. Serum Cr was measured by Modular D following the Jaffe method, and serum Cr was measured by Cobas 8000 c702 and AU5800, following the Jaffe and enzyme methods. Results: All of the total coefficients of variations (CVs) were below 5%. Linearity was observed in the performance ranges evaluated (r>0.99, slope: 0.965 and 0.955). When Modular D and Cobas 8000c 702 were compared, the slope and y-intercept were 0.9928 (95% confidence interval [CI]: 0.9802 to 1.000) and -0.0156 (95% CI: -0.0200 to -0.0054), respectively. The slope and y-intercept were 0.9811 (95% CI: 0.9570 to 0.9951) and -0.0484 (95% CI: -0.0638 to -0.0297) when Modular D and Au5800 were compared. Serum Cr measured by Cobas 8000 c702 and AU5800 using the Jaffe method were 3.2% and 6.9% lower than the values measured by Modular D, respectively. Both Modular D and Cobas 8000 c702 showed acceptable accuracies. Conclusions: Serum Cr measurements using Cobas 8000 c702 and AU5800 were comparable to those measured by Modular D, and showed satisfactory precision and linearity; thus, these techniques could be useful for clinical laboratories. 배경: 혈청 크레아티닌은 신장 기능을 평가하는 대표적인 표지자 이다. 본 연구에서는 Modular D (Roche Diagnostics, Germany) 장 비와 Cobas 8000 c702 (Roche Diagnostics) 및 AU5800 (Beckman Coulter, USA) 장비의 크레아티닌 결과를 비교하였다. 또한, Jaffe법 과 효소법으로 측정한 혈청 크레아티닌 결과의 차이를 비교하였다. 방법: CLSI 지침을 참고하여 정밀도, 직선성, 상관성 평가 등을 수 행하였으며, 100명의 환자 검체를 이용하여 세 종류의 장비에서 혈 청 크레아티닌 값을 측정하였다. Modular D에 의한 혈청 크레아티 닌은 Jaffe법을 사용하여 측정하였고, Cobas 8000 c702 및 AU5800 의 혈청 크레아티닌은 Jaffe법 및 효소법의 두 가지 방법을 사용하 여 각각 측정하였다. 결과: 전체 변이계수는 모두 5% 미만이었으며, 직선성도 우수하였 다. Modular D와 Cobas 8000 c702의 회귀분석 상관식에서 기울기 는 0.9928 (95% 신뢰구간 0.9802~1.0000), Y 절편은 -0.0156 (95% 신뢰구간 -0.0200~-0.0054)였으며, Modular D와 Au5800간 상관식 에서 기울기는 0.9811 (95% 신뢰구간 0.9570~0.9951), Y 절편은 -0.0484 (95% 신뢰구간 -0.00638~-0.0297)이었다. Cobas 8000 c702 와 AU5800에서 Jaffe법으로 측정한 혈청 크레아티닌 측정 결과는 Jaffe법을 이용해 Modular D로 측정한 혈청 크레아티닌 결과에 비 해 각각 평균적으로 3.2%와 6.9% 더 낮은 값을 나타냈다. Modular D와 Cobas 8000 c702는 모두 정확도 평가에서 만족스러운 결과를 보였다. 결론: Cobas 8000 c702와 Beckman Coulter AU5800으로 시행한 혈청 크레아티닌 검사는 정밀도와 직선성에 있어서 만족스러운 성 능을 보였으며, Roche Modular D 검사 결과와 적절한 상관성을 보 여서 임상검사실에 유용할 것이라고 생각한다.
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김도영,신동하,정소라,이종석,조한영,배경숙,성창근,이영하,손광희,박호용 한국미생물학회 2014 The journal of microbiology Vol.52 No.10
The gene (1350-bp) encoding a modular β-1,4-xylanase (XylU),which consists of an N-terminal catalytic GH10 domain anda C-terminal carbohydrate-binding module 2 (CBM 2), fromStreptomyces mexicanus HY-14 was cloned and functionallycharacterized. The purified His-tagged recombinant enzyme(rXylU, 44.0 kDa) was capable of efficiently hydrolyze diversexylosidic compounds, p-nitrophenyl-cellobioside, and pnitrophenyl-xylopyranoside when incubated at pH 5.5 and65°C. Especially, the specific activities (649.8 U/mg and 587.0U/mg, respectively) of rXylU toward oat spelts xylan andbeechwood xylan were relatively higher than those (<500.0U/mg) of many other GH10 homologs toward the samesubstrates. The results of enzymatic degradation of birchwoodxylan and xylooligosaccharides (xylotriose to xylohexaose)revealed that rXylU preferentially hydrolyzed thesubstrates to xylobiose (>75%) as the primary degradationproduct. Moreover, a small amount (4%<) of xylose was detectedas the degradation product of the evaluated xylosidicsubstrates, indicating that rXylU was a peculiar GH10 β-1,4-xylanase with substrate specificity, which was different fromits retaining homologs. A significant reduction of the bindingability of rXylU caused by deletion of the C-terminal CBM2 to various insoluble substrates strongly suggested that theadditional domain might considerably contribute to theenzyme-substrate interaction.
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