Nanoparticle probe ribosome inactivating protein.doc

 PAGE \* MERGEFORMAT 17 Nanoparticle probe ribosome inactivating protein [Abstract] established the nanoparticle probe ribosome inactivating protein approach. Polystyrene nanoparticles as vector and surface modification on the surface of a fixed specificity of ricin and monoclonal antibody as a probe for the grate Ma toxic protein detection. using field flow fractionation techniques for accurate characterization of nanoparticle probes, and by scanning electron microscopy morphology of polystyrene nanoparticles. Results show that: by scanning electron microscopy images of polystyrene nanoparticles could be observed surface binding proteins, the nano-particle probes to work with ricin and other ribosome inactivating protein from specific binding, used in the detection of the target protein. [Keywords:] nanoparticle probe; ricin; ribosome inactivating protein; field flow fractionation; scanning electron microscopy; polystyrene 1 Introduction Ribosome inactivating protein (Ribosome inactivating proteins, RIP) present in many plants, plant ribosome inactivating protein from the defensive role of physiological functions, namely, resistance to pests or harsh environment [1]. According to the protein’s primary structure, RIP can be divided into two categories: Ⅰ type, by a polypeptide; Ⅱ type, is a double-stranded protein. Ⅱ type double-stranded RIP from the two or four polypeptide chains, the molecular weight of about 60 or 120 kDa, one of which is A (Active) chain, with N glycosidase activity; the other is B (Binding) chain, two chains by disulfide bonds and non-covalently linked [2,3]. Ricin is a typical ribosomal inactivating protein, ricin wide variety of sources since the Prohibition of Chemical and Biological Weapons Convention to ricin as the most stringent control [4,5]. Therefore, the conduct of ricin and other ribosome inactivating protein detection significance [6 8]. At present, the ribosome inactivating protein detection methods are immunoassa