Extraction and Purification of Art v 1, the Mugwort Pollen Major Allergen

2007 ◽  
Vol 119 (1) ◽  
pp. S107
Author(s):  
M. Egger ◽  
P. Gruber ◽  
F. Ferreira
2002 ◽  
Vol 17 (1) ◽  
pp. 106-108 ◽  
Author(s):  
Martin Himly ◽  
Beatrice Jahn‐Schmid ◽  
Azra Dedic ◽  
Peter Kelemen ◽  
Nicole Wopfner ◽  
...  
Keyword(s):  

2009 ◽  
Vol 74 (4) ◽  
pp. 359-366 ◽  
Author(s):  
Dragana Stanic ◽  
Lidija Burazer ◽  
Marija Gavrovic-Jankulovic ◽  
Ratko Jankov ◽  
Tanja Cirkovic-Velickovic

Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v 1 that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified amino groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids.


2009 ◽  
Vol 46 (3) ◽  
pp. 416-421 ◽  
Author(s):  
Azra Dedic ◽  
Gabriele Gadermaier ◽  
Lothar Vogel ◽  
Christof Ebner ◽  
Stefan Vieths ◽  
...  

Allergy ◽  
2004 ◽  
Vol 59 (9) ◽  
pp. 995-1001 ◽  
Author(s):  
L. Jimeno ◽  
O. Duffort ◽  
C. Serrano ◽  
D. Barber ◽  
F. Polo

Allergy ◽  
2003 ◽  
Vol 58 (10) ◽  
pp. 1003-1010 ◽  
Author(s):  
R. Bauer ◽  
M. Himly ◽  
A. Dedic ◽  
F. Ferreira ◽  
J. Thalhamer ◽  
...  

1970 ◽  
Vol 63 (2) ◽  
pp. 225-241 ◽  
Author(s):  
B. D. Reeves ◽  
M. L. A. de Souza ◽  
I. E. Thompson ◽  
E. Diczfalusy

ABSTRACT An improved method for the assay of plasma progesterone by competitive protein binding is described. The improvement is based upon rigorous control of the variables, the compensation for and standardisation of interfering factors inherent in the method and the use of a human corticosteroid binding globulin, that meets the requirements for sensitivity at levels of 1.0 ng of progesterone and below. The assessment of the reliability of the individual steps in the method as well as that of the complete method is presented. The sensitivity of the method is around 0.2 ng progesterone per ml plasma. Accuracy was measured by adding progesterone in amounts ranging from 0.0 to 1.0 ng to 1.0 ml plasma. There was a linear relationship between the progesterone added and recovered throughout the entire range of values, with a coefficient of correlation (r) of 0.94. Of 52 related steroids tested, none was found which would remain associated with progesterone following extraction and purification and which would also compete with progesterone for binding sites.


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