| Title: | "Molecular and crystal properties of Bos d 2, an allergenic protein of the lipocalin family" |
| Author(s): | Rautiainen J; Auriola S; Rouvinen J; Kauppinen J; Zeiler T; Novikov D; Virtanen T; Mantyjarvi RA; |
| Address: | "Department of Clinical Microbiology, University of Kuopio, Finland" |
| Journal Title: | Biochem Biophys Res Commun |
| ISSN/ISBN: | 0006-291X (Print) 0006-291X (Linking) |
| Abstract: | "The relationship between the molecular structure of allergenic proteins and the allergenic determinants is one of the central issues in allergology. We report here that the natural preparation of Bos d 2, a mammalian lipocalin allergen, comprises three molecular variant proteins of 17,829, 17,781, and 17,800 Da. When cDNA of Bos d 2 (Genome Sequence Data Base No. L42867) was recloned and expressed in Pichia pastoris, two proteins were produced. One of the proteins (17,831 Da) and the proteins in the natural preparation had pyroglutamate as the N-terminal residue; in the other (17,849 Da) the N-terminal residue was glutamine. Recombinant Bos d 2 protein was crystallized and the native data set was collected at 1.8 A resolution" |
| Keywords: | "Allergens/*chemistry Animals Antigens, Plant Carrier Proteins/*chemistry Cattle Cloning, Molecular Crystallization Crystallography, X-Ray Mass Spectrometry Pheromones/chemistry Pichia/genetics Pyrrolidonecarboxylic Acid/chemistry Recombinant Proteins/chem;" |
| Notes: | "MedlineRautiainen, J Auriola, S Rouvinen, J Kauppinen, J Zeiler, T Novikov, D Virtanen, T Mantyjarvi, R A eng Research Support, Non-U.S. Gov't 1998/07/02 Biochem Biophys Res Commun. 1998 Jun 29; 247(3):746-50. doi: 10.1006/bbrc.1998.8851" |
