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면역글로부린 G 생성에 대한 아이오타 - 카라기난의 어쥬번트 효과
구본웅,이광재,김만석,김하형,Koo, Bon-Woong,Lee, Kwang-Jae,Kim, Man-Suk,Kim, Ha-Hyung 대한약학회 2000 약학회지 Vol.44 No.6
To investigate the effects of iota-carrageenan (CAR) and/or alum on the adjuvancity as well as the structural difference of oligosaccharide on the IgG2b in the adjuvant effect, C57BL/6 mice were immunized twice with fetuin as a model antigen. CAR alone showed no significant effect on induction of antibody except IgG1. In contrast, Alum-CAR (after mixing of antigen-Alum, CAR adjuvant was prepared) and CAR-Alum (after formulation of antigen-CAR, Alum adjuvant was prepared) enhanced production of antibody, especially, IgG2b. After separation of IgG2b, changes of glycosylation were investigated using enzymelinked lectin assay. High affinity of IgG2b to N-acetylneuraminic acid, galactose and mannose-specific lectin were induced by CAR-Alum adjuvant, however, the affinity of IgG2b induced by CAR-Alum to GlcNAc and GalNAc-specific lectin were much less than that induced by Alum-CAR.
윤재경(Jae Kyoung Youn),이영재(Young Jae Lee),구본웅(Bon Woong Koo),윤상영(Sang Young Youn),유창수(Chang Soo Ryu),김하형(Ha Hyung Kim) 대한약학회 2000 약학회지 Vol.44 No.2
The enzymatic properties of beta-galactosidases from Aspergillus oryzae, bovine liver and Saccharomyces fragilis have been studied using enzyme-linked lectin assay based on the RCA120 and BS-II lectins which specifically bind to terminal galactose and G1cNAc residue, respectively. Asialofetuin, a monomeric glycoprotein with approximately 48kDa in molecular weight, was used as a substrate. This glycoprotein contains three N-linked triantennary complex type carbohydrate chains with each of which terminating in Ga1beta1-4GlcNAc (74%). Their optimal pHs were 3.5 and 6.5 (A. oryzae), and 3.5~5.5 (bovine liver and S.fragilis) at 37oC during 24hrs, and the effective concentrations were 0.9, 2.9, and 1.7mg/ml, respectively. The enzyme from A.oryzae requires 100mM Na+ or K+, while the enzyme from bovine liver requires Ba2+ for activity. However all of the three beta-galactosidases were inactivated by SDS and CU2+. These results indicate that the hydrolysis of glycoprotein such as asialofetuin depends on the reaction conditions of beta-galactosidases and some metal ions.