References/Publications for Crossed immunoelectrophoresis of Bet v 1

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2101127 Int Arch Allergy Appl Immunol. 1990;93(4):378-84.

Purification and N-terminal amino acid sequence of two birch pollen isoallergens
(Bet v I and Bet v II).

Elsayed S(1), Vik H.

6886253 J Allergy Clin Immunol. 1983 Aug;72(2):150-9.

Isolation and immunochemical characterization of the major allergen of birch
pollen (Betula verrucosa).

Ipsen H, Løwenstein H.

The classification of some of the extractable birch pollen antigens as allergens
was established by crossed radioimmunoelectrophoresis (CRIE). In CRIE the major
allergen (antigen 23) exhibited the strongest "radiostaining," and only a few
other components of birch pollen extract were visibly radiostained. The major
allergen and a preparation containing mainly the minor allergens, antigens 25 and
19, were isolated from a crude aqueous birch pollen extract by a combination of
anion-exchange, size-exclusion, and chelate chromatography. Antigen 23 was
purified to near homogeneity. The molecular weights and the pIs of antigens 23,
25, and 19 were determined to be 17,000 daltons, pI 5.25 (5.5, 5.0); 25,000
daltons, pI 5.0 (4.9, 5.4); and 29,000 daltons, pI 6.2 (5.4), respectively. The
classification of antigen 23 as the major allergen in birch pollen was supported
by results of RAST inhibition experiments, RAST screening, and skin prick

PMID: 6886253 [Indexed for MEDLINE]
Int Arch Allergy Immunol. 1993;102(3):249-58.

Characterization of recombinant bet vI, the major pollen allergen of Betula
verrucosa (white birch), produced by fed-batch fermentation.

Larsen JN(1), Casals AB, From NB, Strøman P, Ipsen H.