ricin/تسوس سني

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الصفحة 1 من عند 19 النتائج

Plasmonic Metasurfaces Based on Nanopin-Cavity Resonator for Quantitative Colorimetric Ricin Sensing.

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In view of the toxic potential of a bioweapon threat, rapid visual recognition and sensing of ricin has been of considerable interest while remaining a challenging task up to date. In this study, a gold nanopin-based colorimetric sensor is developed realizing a multicolor variation for ricin

In vivo studies of whole ricin monoclonal antibody immunoconjugates for the treatment of murine tumours.

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Ricin is a highly potent toxin which binds to cells via galactose binding sites on the B chain; the toxicity is manifest by the A chain and most studies with immunotoxins have used ricin A chain-antibody conjugates. We have previously described a method for the coupling of whole ricin to monoclonal

Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice.

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RiVax is a candidate ricin toxin subunit vaccine antigen that has proven to be safe in human phase I clinical trials. In this study, we introduced double and triple cavity-filling point mutations into the RiVax antigen with the expectation that stability-enhancing modifications would have a

Lesions of acute inhaled lethal ricin intoxication in rhesus monkeys.

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Five unimmunized adult rhesus monkeys weighing 5.9-6.3 kg were challenged with a precalculated, inhaled dose of 20.95-41.8 micrograms/kg of aerosolized ricin. Two males and three females either died or were killed at the onset of respiratory distress between 36 and 48 hours post-ricin inhalation and

Selective killing of human bladder cancer cells by combined treatment with A and B chain ricin antibody conjugates.

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The monoclonal antibody 486P 3-12-1 raised against transitional bladder carcinoma cells was coupled to either the ricin A or B chain. The toxicity of A chain conjugates could be enhanced by addition of either free ricin B chain or by ricin B chain coupled to 486P 3-12-1 or to antibodies conjugated

Transferrin-ricin A chain toxin limits the development of experimental proliferative vitreoretinopathy.

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This study was designed to determine the safety and efficacy of transferrin-ricin A chain toxin (Tfr-rRA) at preventing retinal detachment in a rabbit model of proliferative vitreoretinopathy (PVR). The toxicity of intravitreal Tfr-rRA (1000-5000 ng) was determined by indirect ophthalmoscopy and

Blocked and not blocked whole-ricin-antibody immunotoxins: intraperitoneal therapy of human tumour xenografted in nude mice.

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A blocked immunotoxin, consisting of ricin and AR-3 monoclonal antibody joined by a short thioether bond, was previously synthesized. This conjugate had lost the ability to bind the galactosidic residues of Sepharose 6B, probably because of the steric restraint of the antibody molecule on the ricin

Monensin in lipid emulsion for the potentiation of ricin A chain immunotoxins.

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The utilization of carboxylic ionophores such as monensin for immunotoxin potentiation may be hampered by the poor solubility and short in vivo half-life of these highly lipophilic compounds. Therefore, the use of monensin formulated in a lipid/water emulsion was investigated for the in vitro and in

X-ray structure of gelonin at 1.8 A resolution.

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Gelonin is a single chain ribosome inactivating protein (RIP) with potential application in the treatment of cancer and AIDS. Diffraction quality crystals grown using PEG3350, belong to the space group P21, with a = 49.4 A, b = 44.9 A, c = 137.4 A and beta = 98.4 degrees, and contain two molecules

Synaptic substrates for enkephalinergic and serotoninergic interactions with dental primary afferent terminals in trigeminal subnucleus interpolaris: an immunocytochemical study using peroxidase and colloidal gold.

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Pain processing in the trigeminal complex has been thought to reside primarily in the spinal subnucleus caudalis (Vc). However, trigeminal tractotomies eliminating primary afferent input to Vc and severance of secondary trigemino-thalamic fibers from Vc do not disturb pain perception from the

NIM-R7, a novel marker for resting B1 and marginal-zone B lymphocytes, is also expressed on activated T and B cells.

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In mice, follicular B cells have been studied in detail, while two other B-cell subpopulations - marginal-zone B and B1 cells - are less well understood. In this work we report the expression pattern of p58, a lymphocyte-activation marker, recognized by rat monoclonal antibody, NIM-R7, and present

Deafferentation-induced alterations in the rat dorsal horn: II. Effects of selective poisoning by pronase of the central processes of a peripheral nerve.

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Studies of deafferentation and regeneration, as well as studies requiring several tracing techniques, would benefit from availability of a substance that would selectively lesion the central components of a single peripheral nerve. Pronase, a combination of proteolytic enzymes, was tested for this

Immunotoxins to the murine transferrin receptor: intracavitary therapy of mice bearing syngeneic peritoneal tumors.

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Two rat monoclonal antibodies to the murine transferrin receptor (TFR) were each conjugated to recombinant ricin toxin A chain (rRTA). The monoclonal antibodies, R17 217 and YE1/9.9, bound to partially overlapping antigenic determinants on the murine TFR that were distinct from the transferrin

Role of intrachain disulfides in the activities of the CdtA and CdtC subunits of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans.

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The cytolethal distending toxin (Cdt) of Actinobacillus actinomycetemcomitans is an atypical A-B-type toxin consisting of a heterotrimer composed of the cdtA, cdtB, and cdtC gene products. The CdtA and CdtC subunits form two heterogeneous ricin-like lectin domains which bind the holotoxin to the

Recognition intensities of submolecular structures, mammalian glyco-structural units, ligand cluster and polyvalency in abrin-a-carbohydrate interactions.

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Abrin-a is the most toxic fraction of lectins isolated from Abrus precatorius seeds and belongs to the family of type 2 ribosome inactivating proteins (RIP). This toxin may act as a defense molecule in plants against viruses, fungi and insects, where attachment of abrin-a to the exposed glycans on

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