• Title/Summary/Keyword: Chemical assay

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Improved Soil Application Bioassay for Efficient Development of Natural Pre-emergence Herbicides (토양처리용 천연물제초제 개발을 위한 생물검정법 개선)

  • Kim, Jae-Deog;Hwang, Hyun-Jin;Seo, Bo-Ram;Choi, Jung-Sup;Kim, Jin-Seog
    • Korean Journal of Weed Science
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    • v.31 no.3
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    • pp.229-239
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    • 2011

  • This study was carried out to establish an improved bioassay system on the side of practicality, pre-emergence bioassay which is more effective in developing soil application natural herbicides. A miniaturized method which have a 50 cm2 of soil surface area and was efficient by 7 times compared to the existing soil application assay ($350cm^2$ of soil surface area) was established, in which four weed species (Echinochloa crus-galli, Digitaria sanguinalis, Aeschynomene indica, and Abutilon theophrasti) were planted and grown in greenhouse. This would be applicable when the amount of screening compound is much more than 50 mg. The initial application rate was desirable at $10,000{\mu}g\;mL^{-1}$. On the other hand, the 6 well plate assay which has 4 weed species in each well containing upland soil and could be conducted in growth chamber, was established. This assay was resulted in minimizing in level of 1/14 test volume and 1/14 amounts of test compound to the conventional method that has been used for screening of synthetic compounds in KRICT, and applicable for the small amount of test compound (less than 10 mg). Therefore, the improved bioassays established in this study would be helpful for a rapid and efficient development of soil application natural herbicides.

  • https://doi.org/10.5660/KJWS.2011.31.3.229 인용 PDF KSCI

Effect of nitrogen compounds on the chemical composition and biological activity of mainstream smoke (질소 화합물이 담배연기성분 및 안전성에 미치는 영향)

  • Shin, Han-Jae;Park, Chul-Hoon;Sohn, Hyung-Ok;Lee, Hyeong-Seok;Kim, Yong-Ha;Hyun, Hak-Chul
    • Journal of the Korean Society of Tobacco Science
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    • v.31 no.2
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    • pp.75-84
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    • 2009

  • The objective of this study was to investigate the effect of nitrogen compounds such as protein on the chemical composition and toxicity of cigarette mainstream smoke. BSA protein was treated into the tobacco leaf of original 2R4F cigarette at 1~4 % level. The studies were performed which included a bacterial mutagenicity assay and a mammalian cell cytotoxicity assay for total particulate matter(TPM), and glutathione(GSH) consumption assay for gas/vapor phase(GVP) and determination of smoke chemical constitute. Cigarettes treated with protein were observed dose-dependent increase in yield of volatiles, semi-volatiles and aromatic amines compared with control cigarette. However, carbonyl compounds such as acrolein was lower than that of control cigarette when calculated on an equal TPM basis. The cytotoxicity of TPM obtained from the protein-added cigarettes was not different from that of control cigarette. However, the mutagenicity of the TPM from protein-treated cigarettes(1~4 %) was up to 10-27 % higher than that of control. On the other hand, toxicity of GVP from protein-treated cigarette(4 %) was significantly decreased compared with control cigarette. An overall assessment of our data suggests that nitrogen compounds such as protein should be important for the chemical composition and biological activity of cigarette mainstream smoke.

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Quantitative Assay of Recombinant Hepatitis B Surface Antigen by Using Surface Plasmon Resonance Biosensor (Surface plasmon resonance 바이오센서를 이용한 재조합 B형 간염 표면항원의 정량분석)

  • Lee, E. K.;Ahn, S. J.;Yoo, C. H.;Ryu, K.;Jeon, J. Y.;Lee, H. I.;Choi, S. C.;Lee, Y. S.
    • KSBB Journal
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    • v.17 no.1
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    • pp.20-25
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    • 2002

  • We performed a basic experiment for rapid, on-line, real-time measurement of HBsAg by using a surface plasmon resonance biosensor to quantify the recognition and interaction of biomolecules. We immobilized the anti-HBsAg polyclonal antibody to the dextran layer on a CM5 chip surface which was pre-activated by N-hydroxysuccinimide for amine coupling. The binding of the HBsAg to the immobilized antibody was measured by the mass increase detected by the change in the SPR signal. The binding characteristics between HBsAg and its antibody followed typical monolayer adsorption isotherm. When the entire immobilized antibody was interacted, there was no additional, non-specific binding observed, which suggested the biointeraction was very specific as expected and independent of the ligand density. No significant steric hindrance was observed at 17.6 nm/$mm^2$ immobilization density. The relationship between the HBsAg concentration in the sample solution and the antigen bound to the chip surface was linear up to ca. $40\mu\textrm{g}$/mL, which is much wider than that of the ELISA method. It appeared the antigen-antibody binding was increased as the immobilized ligand density increased, but verification is warranted. This study showed the potential of this biosensor-based method as a rapid, simple, multi-sample, on-line assay. Once properly validated, it can serve as a more powerful method for HBsAg quantification replacing the current ELISA method.

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