References/Publications for Radio Immunoassay of Ant o 1

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2434841 Mol Immunol. 1986 Dec;23(12):1281-8.

Monoclonal antibodies to the major Lolium perenne (rye grass) pollen allergen Lol
p I (Rye I).

Kahn CR, Marsh DG.

Thirteen monoclonal antibodies (MAbs) were produced against Lol p I (Rye I), the
major Lolium perenne (rye grass) pollen allergen. Spleen cells from A/J and SJL
mice immunized with highly purified Lol p I (Lol I) were allowed to fuse with
cells from the non-secreting Sp2/0-Ag14 myeloma cell line. Each MAb was analyzed
for antigenic specificity by radioimmunoassay (RIA) using 125I-Lol I. The epitope
specificities of seven of the MAbs were examined by competitive binding against a
labelled standard MAb for the Lol I antigen (Ag). The dissociation constant, Kd,
of one MAb (No. 3.2) that was studied most extensively was determined by double
Ab RIA to be 3.5 X 10(-6) L/M. This MAb recognized the related 27,000-30,000
Group I glycoproteins found in the pollens of nine other species of grass pollens
tested, including weak binding to Bermuda grass Group I (Cyn d I), which by
conventional analysis using polyclonal anti-Lol I serum shows no detectable
binding. Monoclonal antibody No. 3.2 was coupled covalently to Sepharose 4B and
used to prepare highly purified Lol I from a partially purified rye pollen
extract. Finally, an RIA was developed which permitted the analysis of the Group
I components in rye grass and nine other grass pollen species. The latter assay
is likely to prove useful in the standardization of grass pollen extracts
according to their Group I contents.

PMID: 2434841 [Indexed for MEDLINE]