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Expression of Difficult-to-Express Proteins, Human IL-12 and IFN-<i>γ</i>
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作者 Yoshihito Hosaka Shun Matsutani +9 位作者 Shinya Kawate Kei Itoh Atsuko Miura Yukaze Mizoura Sayumi Yamada Seiya Uemura Hiroshi Konno Ewa Grave hideki wakui Hideaki Itoh 《American Journal of Molecular Biology》 2021年第2期29-37,共9页
It is known to be that lactic acid bacteria induce the IL-12. IL-12 activates NK cells and promotes the production of IFN-<em>γ</em>. IFN-<em>γ</em> activates macrophages, resulting in enhanc... It is known to be that lactic acid bacteria induce the IL-12. IL-12 activates NK cells and promotes the production of IFN-<em>γ</em>. IFN-<em>γ</em> activates macrophages, resulting in enhanced phagocytosis and bactericidal activity. We have been investigating fermented foods that activate the immune function. For that purpose, a specific antibody is required. We tried to express IL-12p35 by the usual method, but IL-12p35 was not expressed at all. In the present study, we constructed, purified human IL-12p35 and obtained a specific antibody against IL-12p35. We also purified human IFN-<em>γ</em> and obtained specific antibody against IFN-<em>γ</em>. We have established a method for expressing poorly expressed proteins. The method we have established can be applied to the purification of poorly expressed proteins and antibody production. 展开更多
关键词 Difficult-to-Express Proteins IL-12 IFN-γ PURIFICATION Antibody Production
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The ATPase activity of molecular chaperone HSP60 is inhibited by immunosuppressant mizoribine 被引量:1
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作者 Masako Tanabe Ryuichi Ishida +6 位作者 Fumiko Izuhara Atsushi Komatsuda hideki wakui Kenichi Sawada Michiro Otaka Nobuhiro Nakamura Hideaki Itoh 《American Journal of Molecular Biology》 2012年第2期93-102,共10页
The molecular chaperone HSP60 is a chaperonin homolog of GroEL. We had previously shown that the immunosuppressant mizoribine is bound directly to HSP60 and inhibited its chaperone activity. However, the inhibitory me... The molecular chaperone HSP60 is a chaperonin homolog of GroEL. We had previously shown that the immunosuppressant mizoribine is bound directly to HSP60 and inhibited its chaperone activity. However, the inhibitory mechanisms of HSP60 by mizoribine have not yet been fully understood. In the present study, we investigated the influence of mizoribine on a folding cycle of HSP60 and co-chaperone HSP10. Our results showed that mizoribine inhibited the folding cycle of HSP60/HSP10. The ATPase activity of HSP60/HSP10 was decreased in the presence of mizoribine and the dissociation of HSP10 from HSP-60 was also decreased by mizoribine. The same functions of GroEL and/or GroES were slightly affected by mizoribine. Based on our findings, we discuss the inhibitory mechanisms of HSP60 by mizoribine. 展开更多
关键词 HSP60 GROEL MIZORIBINE INHIBITION MECHANISMS Conformational Change
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