Crossed Radioimmunoelectrophoretic Analysis of Cultivated Rye &lt;i&gt;(Secale cereale) &lt;/i&gt;Pollen Allergens

Renck, B.; Einarsson, R.

doi:10.1159/000233466

Cited by 6 publications

(1 citation statement)

References 10 publications

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“…Comparing the results obtained in this study to those achieved by CRIE [21,28] using the same amount of allergen, Immunoprint proves to be better in terms of time needed (1 day versus several days) and numbers of allergens recognized (more than 30 versus 16). Furthermore, there is no need to use radiolabeled second antibodies [36].…”

Section: Discussionmentioning

confidence: 53%

Analysis of Rye Pollen <i>(Secale cereale)</i> Allergens Using Patients’ IgE, Immunoprint, Western Blot and Monoclonal Antibodies

Westphal¹,

Becker²,

Schlaak³

1988

Int Arch Allergy Immunol

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Rye pollen (Secale cereale) was investigated by Immunoprint and Western Blot analysis. Using Immunoprint, more than 30 proteins could be shown to be allergens in terms of their IgE binding, and 9 were determined as major allergens. In Western Blot 17 allergens were discovered, 3 of them major allergens. 4 monoclonal antibodies raised against a pollen extract of 6 grasses showed cross-reactivity to rye pollen, thus indicating common epitopes. 1 of 3 monoclonal antibodies produced against an extract of rye pollen was only reacting to this pollen. Looking at the overall binding pattern of the 7 monoclonal antibodies, they showed partial identity to patients’ IgE in Immunoprint and Western Blot. The possibility of defining epitopes using preparative isolelectric focusing and monoclonal antibodies is discussed.

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Section: Discussionmentioning

confidence: 53%

Analysis of Rye Pollen <i>(Secale cereale)</i> Allergens Using Patients’ IgE, Immunoprint, Western Blot and Monoclonal Antibodies

Westphal¹,

Becker²,

Schlaak³

1988

Int Arch Allergy Immunol

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An immunoelectrophoretic analysis of the allergens of Cynodon dactylon (Bermuda grass) pollen

Matthiesen

Schumacher

Løwenstein

1989

Journal of Allergy and Clinical Immunology

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Group V allergens in grass pollens. I. Purification and characterization of the group V allergen from Phleum pratense pollen, Phl p V

Matthiesen

Løwenstein

1991

Clin Experimental Allergy

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An allergen from Phleum pratense (timothy) pollen, Phl p V, has been isolated by a combination of copper chelate affinity chromatography and ion exchange chromatography. Phl p V binds IgE from serum of grass-sensitized donors as revealed in immunoelectrophoretic techniques and in SDS-PAGE immunoblot, and luminescence immunoassay (LIA) inhibition experiments indicate that the allergen represents a significant part of the IgE binding capacity of the extract. In immunoelectrophoresis, Phl p V is revealed as a single precipitate. However, molecular weight studies show that Phl p V consists of at least two isoforms with similar immunochemical properties, but with different molecular size. After SDS-PAGE treatment purified Phl p V is identified as two IgE-binding components, Phl p Va and Phl p Vb, with molecular weights 33 and 29 kD. After HPLC gel filtration, Phl p Va and Phl p Vb are identified in the major 30-kD eluate. After Sephadex G75 gel filtration of whole pollen extract, Phl p V is identified in fractions corresponding to molecular weights 47 and 25 kD. The 47-kD fraction corresponds to Phl p Va/Phl p Vb as seen in SDS-PAGE, while the 25-kD component presumably corresponds to a degradation product present in whole pollen extract. The NH2-terminal sequence of Phl p V, corresponding to approximately 10% of the molecule, has been determined. The sequence shows minor variations in some residues and contains besides many alanine residues also hydroxyproline; the sequence reveals no homologies to any known NH2 terminal sequence of other proteins. The amino acid composition, revealing 26 mole % alanine and no cysteine, does not show any similarities to other known amino acid compositions of allergens. From the amino acid composition determination and an immunoelectrophoretic comparison, Phl p V is estimated to represent 6% (w/w) of the whole pollen extract.

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Crossed Radioimmunoelectrophoretic Analysis of Cultivated Rye <i>(Secale cereale) </i>Pollen Allergens

Cited by 6 publications

References 10 publications

Analysis of Rye Pollen <i>(Secale cereale)</i> Allergens Using Patients’ IgE, Immunoprint, Western Blot and Monoclonal Antibodies

Analysis of Rye Pollen <i>(Secale cereale)</i> Allergens Using Patients’ IgE, Immunoprint, Western Blot and Monoclonal Antibodies

An immunoelectrophoretic analysis of the allergens of Cynodon dactylon (Bermuda grass) pollen

Group V allergens in grass pollens. I. Purification and characterization of the group V allergen from Phleum pratense pollen, Phl p V

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