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[Heidenhain's variant of Creutzfeldt-Jakob's disease].
Rev Neurol (Paris)
May 2005
Unite de Neuro-ophtalmologie et service de Neurologie D, Hospices Civils de Lyon, Hôpital Neurologique Pierre-Wertheimer, Bron.
Introduction: Creutzfeldt-Jakob's disease has various anatomoclinical presentations including a rare form with preponderant visual signs described by Heidenhain. In this form, the visual symptoms may be isolated for a few weeks, leading to multiple ophthalmological examinations.
Observation: We report the case of a 75-year-old woman who developed isolated visual disorders which rapidly increased over a period of two months.
Isolation and characterization of an acetyl group-recognizing agglutinin from the serum of the Indian white shrimp Fenneropenaeus indicus.
Arch Biochem Biophys
June 2002
Laboratory of Pathobiology, Department of Zoology, University of Madras, Guindy Campus, Chennai 600 025, India.
A natural agglutinin from the serum of the Indian white shrimp Fenneropenaeus (Penaeus) indicus was purified to electrophoretic homogeneity by a single-step affinity chromatography on N-acetylglucosamine-Sepharose 6B. The expression of hemagglutinating (HA) activity of F. indicus agglutinin (FIA) was independent of the presence of divalent cations and insensitive to their chelators.
View Article and Find Full Text PDF[Antigenic identity of the capsule lipopolysaccharides, exopolysaccharides, and O-specific polysaccharides in Azospirillum brasilense].
Mikrobiologiia
July 2002
Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, pr. Entuziastov 13, Saratov, 410015 Russia.
The antigenic identity (and close values of electrophoretic mobility) of capsular polysaccharides, exopolysaccharides, and O-specific polysaccharides was revealed in the Azospirillum brasilense strains Sp7 and Sp245 by the immunodiffusion and immunoelectrophoretic methods. Together with the literature data on the identity of the monosaccharides composition of these polymers, this gives evidence of the absence of a specific capsular antigen in the bacteria studied. Thus, extracellular Azospirillum brasilense polysaccharides are likely to represent O-antigenic lipopolysaccharide fragments excreted by the bacteria into the culture medium, and their identification as a capsule or as an exopolysaccharide depends on the strength of the attachment of these polysaccharides to the cell surface.
View Article and Find Full Text PDFImmunoglobulin G class identification from wild ungulates by cross-reactivity with antisera to domestic animals.
J Vet Med B Infect Dis Vet Public Health
August 2000
Servicio de Ecopatología de Fauna Silvestre, Facultad de Veterinaria, Universidad Autónoma de Barcelona, Spain.
Seven species of Spanish ungulates were tested for the presence of homologous immunoglobulin G (IgG) with a gel-diffusion test using bovine, ovine, caprine and porcine IgG antisera. Homologous ovine and caprine IgG were detected in sera from chamois (Rupicapra pyrenaica), Spanish ibex (Capra pyrenaica hispanica), mouflon (Ovis orientalis musimon), red deer (Cervus elaphus), fallow deer (Dama dama) and roe deer (Capreolus capreolus). Homologous porcine IgG was detected in wild boar (Sus scrofa) serum.
View Article and Find Full Text PDFDifferentiation of cultured brown adipocytes is associated with a selective increase in the short variant of g(s)alpha protein. Evidence for higher functional activity of g(s)alphaS.
Mol Cell Endocrinol
September 2000
Institute of Physiology, Czech Academy of Sciences, Videánská 1083, 142 20 4, Prague, Czech Republic.
In order to examine whether the differentiation process in brown adipocytes cultivated in primary culture is associated with substantial alterations in the complement of G proteins, the levels of these proteins were investigated with immuno-electrophoretic techniques in membrane preparations from proliferating and differentiated cultured mouse brown adipocytes. We observed that differentiation was associated with a dramatic (more than threefold) increase in the short variant of G(s)alpha protein (G(s)alphaS). The long variant of G(s)alpha (G(s)alphaL), as well as G(i)1alpha, G(i)2alpha, G(q)alpha, G(11)alpha and Gbeta subunit proteins remained unchanged whereas G(i)3alpha protein was decreased.
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