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glucose Oxidase 효소전극 제조 화학적 방법에 의한 효소의 고정화
전재현,권형주,한미영,김두식 ( Jae Hyeon Juhn,Hyoung Joo Kwon,Mi Young Han,Doo Sik Kim ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.1
Glucose oxidase was purified from Penicillium verruculosum, and immobilized by various chemical methods such as crosslinking of the enzyme with BSA by glutaral dehyde, covalent coupling with ω-aminohexyl agarose via glutaraldehyde as a bifunctional spacer group or covalent attachment of ω-aminohexyl agarose and the enzyme by amide bond. Construction of the enzyme electrode was carried out using the immobilized glucose oxidase, and the catalytic parameters as well as functional stability of the immobilized enzyme were monitored by oxygen electrode. Optimal pH of the glucose oxidase activity was shifted toward neutral side with more extended pH range as a result of immobilization and thermal stability of the catalytic function was also greatly improved compared to that of soluble enzyme. Practical application of the enzyme electrode for the determination of glucose concentration in biological fluids is demonstrated.
YHB6211(recombinant human granulocyte-colony stimulating factor)의 토끼에서 국소자극성에 관한연구
최연식(Yeon Shik Choi),안경규(Kyoung Kyu Ahn),전재현(Jae Hyeon Juhn),이종성(Jong Sung Lee),문병석(Byoung Seok Moon),유광현(Kwang Hyun You) 한국독성학회 1999 Toxicological Research Vol.15 No.2
Local irritation of YHB6211, a recombinant human granulocyte-colony stimulating factor, was assessed in male New Zealand White (NZW) rabbits by dermal and ocular application. In the skin irritation test, 0.5 ml of 0.03% YHB6211 aqueous solution was applied to the back skin of rabbits for 24 hours, and subsequent observation was performed. The solution did not induce any response after the treatment, and the primary irritation index (P.I.I.) of the compound was 0. In the eye irritation test, 0.1 ml of the same solution was instilled into the conjunctiva of the eye. No treatment related reactions were observed at the cornea, iris, and conjunctiva. Based on these results, 0.03% (w/v) YHB6211 solution could be considered as a non-irritating material.
시리안 햄스터 볼주머니 점막에 대한 recombinant human Granulocyte Macrophge-Colony Stimulating Factor의 효과
조선아(Sun-A Cho),박종환(Jong-Hwan Park),석승혁(Seung-Hyeok Seok),전재현(Jae-Hyeon Juhn),김성진(Seong-Jin Kim),지희정(Hyi-Jeong Ji),추연성(Youn-Sung Choo),박재학(Jae-Hak Park) 한국실험동물학회 2004 Laboratory Animal Research Vol.20 No.3
This study was aimed to identify the effect of recombinant human Granulocyte Macrophge-Colony Stimulating Factor (rhGM-CSF) on the mucous membrane of hamster cheek pouch. After anesthetized with ketamine and xylazine, hamsters were topically administered with rhGM-CSF at the dose of 0.4 ㎍/㎖, 2㎍/㎖, 10 ㎍/㎖, 50 ㎍/㎖, and 250 ㎍/㎖ for 14 days. The thickness of the sratum basale, stratum spinosum, and stratum corneum was determined in each group. And cell proliferation in mucosal layer was also evaluated by immunohistochemistry. The thickness of stratum spinosum increased in the group administered with rhGM-CSF of 0.4 ㎍/㎖ (1.75㎛±0.69), but decreased in the groups administered with that of over 2 ㎍/㎖. In immunohistochemistry, high Ki-67 positive response was also detected in the hamster administered with rhGM-CSF of 0.4㎍/㎖. This study showed that rhGM-CSF induces the epithelial proliferation at concentration of 0.4㎍/㎖.
glucose Oxidase 효소전극 제조 : 화학적 방법에 의한 효소의 고정화 Immobilization of enzyme by chemical methods
김두식,한미영,전재현,권형주 생화학분자생물학회 1993 BMB Reports Vol.17 No.3
Glucose oxidase was purified from Penicillium verruculosum, and immobilized by various chemical methods such as crosslinking of the enzyme with BSA by glutaral dehyde, covalent coupling with ω-aminohexyl agarose via glutaraldehyde as a bifunctional spacer group or covalent attachment of ω-aminohexyl agarose and the enzyme by amide bond. Construction of the enzyme electrode was carried out using the immobilized glucose oxidase, and the catalytic parameters as well as functional stability of the immobilized enzyme were monitored by oxygen electrode. Optimal pH of the glucose oxidase activity was shifted toward neutral side with more extended pH range as a result of immobilization and thermal stability of the catalytic function was also greatly improved compared to that of soluble enzyme. Practical application of the enzyme electrode for the determination of glucose concentration in biological fluids is demonstrated.