Zobrazeno 1 - 10
of 53
pro vyhledávání: '"J. Rabillon"'
Autor:
Pascal Poncet, Jean-Marc Laval, Thierry Fontaine, Bernard David, J. Rabillon, Hany Goubran Botros
Publikováno v:
European Journal of Biochemistry. 268:3126-3136
A new allergen from horse dander, Equ c 5 has been purified. Its biochemical and biophysical properties have been characterized and compared with those of Equ c 1, Equ c 2 and Equ c 4. Their molecular masses, determined by mass spectrometry, were 22
Autor:
Bernard David, Jean-Claude Mazie, Gisele A. Tavares, Pedro M. Alzari, Isabelle Rosinski-Chupin, Pascal Poncet, J. Rabillon, Hany Goubran-Botros, Christophe Grégoire, Marie-Bernard Lascombe
Publikováno v:
Journal of Biological Chemistry. 275:21572-21577
The three-dimensional structure of the major horse allergen Equ c 1 has been determined at 2.3 A resolution by x-ray crystallography. Equ c 1 displays the typical fold of lipocalins, a β-barrel flanked by a C-terminal α-helix. The space between the
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 710:57-65
Purification of two allergens from horse (Equus caballus) sweat, Equ c2 and Equ c3, by means of salt-promoted chromatography on a "thiophilic" (T-gel) adsorbent is described. Immobilization of these proteins was found to be dependent on the presence
Publikováno v:
Immunology. 88:340-347
Horse serum albumin is present in the near vicinity of the animal, while dog and cat serum albumins are very common allergens present in house dust. Human patients clinically defined as allergic to horse could react with horse serum albumin by means
Publikováno v:
Revue Française d'Allergologie et d'Immunologie Clinique. 35:519-523
Resume Nous avons essaye d'apporter un certain nombre d'arguments theoriques, et experimentaux a l'appui de l'hypothese selon laquelle il pourrait exister une relation entre la structure, la fonction et l'allergenicite de certaines proteines d'origin
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 621:23-31
Equ.cl, the horse (Equus caballus) major allergen, was identified in a partially purified extract obtained from a crude aqueous horse dander extract, by acetonic precipitation and a salting-out process. It was isolated and purified by size-exclusion
Publikováno v:
Immunology Letters. 33:229-232
Mice of 6 strains were immunized with a highly purified Fel dI allergen adsorbed to alum. Their ability to display a significant IgE response was detected via passive cutaneous anaphylaxis (PCA) tests, performed in rats. Linkage of the responsiveness
Publikováno v:
Journal of Chromatography A. 539:475-484
Proteins, regardless of their origin, have to be highly purified, particularly from the immunochemical point of view, if they are to be used to study their allergenicity. It is shown that cat albumin, a highly potent allergen for cat-sensitive humans
Publikováno v:
Journal of Chromatography A. 512:177-188
Although the efficient isolation and purification of the major feline allergen have previously been achieved using polyclonal or monoclonal antibody affinity chromatography these methods lead to a relatively low yield of pure allergen. Therefore, att
Publikováno v:
European journal of biochemistry. 268(10)
A new allergen from horse dander, Equ c 5 has been purified. Its biochemical and biophysical properties have been characterized and compared with those of Equ c 1, Equ c 2 and Equ c 4. Their molecular masses, determined by mass spectrometry, were 22