References/Publications for Chromatography of Der p 1

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7048069 Mol Immunol. 1982 Feb;19(2):339-46.

Purification of a murine IgE-inducing antigen extracted from the house dust mite,
Dermatophagoides pteronyssinus.

Abe T, Ishii A.

A major antigen inducing IgE in mice (DpI) was purified from a crude extract of
Dermatophagoides pteronyssinus (D.p.) using Sephacryl S-200 gel filtration, DE52
ion exchange chromatography and isoelectric focusing. This antigen is not one of
the major D.p. human allergens. Isoelectric focusing showed a single peak of PCA
activity at pI 4.7. Activity followed a broader banding pattern on polyacrylamide
gel electrophoresis (PAGE). The molecular weight of DpI estimated from Sephadex
G-150 chromatography was 1.7 X 10(5) daltons. Molecular weight calculated from
SDS-gels (reducing), however, was 3.7 X 10(4), which may indicate a molecule with
a subunit composition. DpI contained no detectable hexose as measured by the
phenol-sulfuric acid assay. PCA activity of DpI was stable at 98 degrees C and to
treatment with 0.1 M sodium metaperiodate, but destroyed by pronase. DpI
represents approximately one per cent of the total protein of crude extracts.
Purified DpI displays a specific activity increase of 40 times that of the crude
extract with the PCA test. DpI is capable of inhibiting 40% of the binding
between crude extract and human IgE, but only at extremely high concentrations.
Human IgE was 700 times more sensitive to D.p. crude extract than purified DpI by
enzyme immunoassay.


PMID: 7048069 [Indexed for MEDLINE]
2911558
Protein Seq Data Anal. 1989;2(1):17-21.

Structural studies on the allergen Der p1 from the house dust mite
Dermatophagoides pteronyssinus: similarity with cysteine proteinases.

Simpson RJ(1), Nice EC, Moritz RL, Stewart GA.


1618983 J Chromatogr. 1992 May 22;599(1-2):105-11.

Isolation of Der pI, the Dermatophagoides pteronyssinus major mite allergen, from
a crude mite culture extract, purification by ion-chromatography, and comparison
between the material obtained and a cDNA-coded Der pI.

Dandeu JP(1), Rabillon J, Lux M, David B, Guillaume JL, Camoin L.


9061221 Clin Exp Allergy. 1997 Feb;27(2):201-7.

Heterogeneous proteolytic specificity and activity of the house dust mite
proteinase allergen Der p I.

Hewitt CR(1), Horton H, Jones RM, Pritchard DI.


15707969 Biochem Biophys Res Commun. 2005 Mar 25;328(4):944-52.

Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine
protease activity.

Takai T(1), Kato T, Sakata Y, Yasueda H, Izuhara K, Okumura K, Ogawa H.


15753904 J Allergy Clin Immunol. 2005 Mar;115(3):555-63.

Analysis of the structure and allergenicity of recombinant pro- and mature Der p
1 and Der f 1: major conformational IgE epitopes blocked by prodomains.

Takai T(1), Kato T, Yasueda H, Okumura K, Ogawa H.


19226276 Clin Exp Allergy. 2009 May;39(5):760-70. doi: 10.1111/j.1365-2222.2009.03201.x.
Epub 2009 Feb 18.

Production of native and modified recombinant Der p 1 molecules in tobacco
plants.

Burtin D(1), Chabre H, Olagnier B, Didierlaurent A, Couret MN, Comeau D, Wambre
E, Laparra H, Van Overtvelt L, Montandon F, Batard T, Jonval V, Lorphelin A,
Merle C, Berrouet C, Parry L, Gomord V, Van Ree R, Moingeon P.


26994626 Asian Pac J Allergy Immunol. 2016 Mar;34(1):51-8. doi: 10.12932/AP0670.34.1.2016.

Allergenicity of native and recombinant major allergen groups 1 and 2 of
Dermatophagoides mites in mite sensitive Thai patients.

Sookrung N(1), Choopong J, Seesuay W, Indrawattana N, Chaicumpa W, Tungtrongchitr
A.