›› 2009, Vol. 52 ›› Issue (1): 27-32.
• RESEARCH PAPERS • Previous Articles Next Articles
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Abstract: One kind of β-1,3-glucan recognition protein (Tm-βGRP) was purified from Tenebrio molitor larvae by such traditional means as neutral salt precipitation and gel chromatography, etc., and its biological functions in pro-phenoloxidase activation system were primarily studied. The results showed that the molecular weight of Tm-βGRP was approximately 70 kDa, and the protein mainly existed in plasma. Purified Tm-βGRP could only specifically recognize β-1,3-glucan, but not peptidoglycan. During the process of pro-phenoloxidase activation induced by β-1,3-glucan, with the proceeding of pro-phenoloxidase activation, the amount of endogenous Tm-βGRP decreased significantly. The polyclonal antibody against Tm-βGRP could inhibit phenoloxidase activity in the hemolymph of T. molitor induced by β-1, 3-glucan in a dose-dependent manner. This research may help us deeply elucidate the biological function of β-1, 3-glucan in pro-phenoloxidase activation system in the hemolymph of T. molitor.
Key words: Tenebrio molitor, β-1, 3-glucan recognition protein, isolation and purification, biological function, pro-phenoloxidase activation system, innate immunity
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http://www.insect.org.cn/EN/Y2009/V52/I1/27
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