These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Two-dimensional gel electrophoretic analyses of Kentucky bluegrass and rye grass pollen allergens. Detection with a murine monoclonal anti-Poa p I antibody and amino terminal amino acid sequence of Poa p I allergen.
    Author: Ekramoddoullah AK.
    Journal: Int Arch Allergy Appl Immunol; 1990; 93(4):371-7. PubMed ID: 2101126.
    Abstract:
    Allergenic extracts of Kentucky bluegrass (Poa pratensis) and rye grass (Lolium perenne) pollen were shown by 2-dimensional (2-D) gel electrophoresis to consist of several hundred protein components. The pollen extracts of the two related grasses had unique 2-D gel patterns. Two major grass pollen allergens, Poa p I and Lol p I, and their isoforms (i.e. isoallergens) were detected and localized on 2-D gels by immunoblotting with anti-Poa p I antibody mAb 60. Poa p I isoallergens were less acidic than Lol p I isoallergens. The relative proportion of four Poa p I isoallergens was (in decreasing pI): A, 13%; B, 37%; and D, 15%. The amino terminal amino acid sequences of the two major isoallergens of Poa p I were identical. However, the amino acid composition of these isoallergens showed enough differences to account for their charge differences. The amino terminal amino acid sequence of two major Poa p I isoallergens had a 70% homology in 20 amino acid overlap with the previously published amino terminal amino acid sequence of rye grass pollen allergen R-7.
    [Abstract] [Full Text] [Related] [New Search]