References/Publications for Chromatography of Ara h 1

Check all              

Select PubMed ID Description
1880317 J Allergy Clin Immunol. 1991 Aug;88(2):172-9.

Identification of a major peanut allergen, Ara h I, in patients with atopic
dermatitis and positive peanut challenges.

Burks AW(1), Williams LW, Helm RM, Connaughton C, Cockrell G, O'Brien T.

7513004 J Allergy Clin Immunol. 1994 Apr;93(4):743-50.

Epitope specificity and immunoaffinity purification of the major peanut allergen,
Ara h I.

Burks AW(1), Cockrell G, Connaughton C, Helm RM.

9677140 Clin Exp Allergy. 1998 Jun;28(6):743-51.

Identification and partial characterization of multiple major allergens in peanut

de Jong EC(1), Van Zijverden M, Spanhaak S, Koppelman SJ, Pellegrom H, Penninks

9988715 J Biol Chem. 1999 Feb 19;274(8):4770-7.

Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not
affect its allergenic properties.

Koppelman SJ(1), Bruijnzeel-Koomen CA, Hessing M, de Jongh HH.

15080811 Clin Exp Allergy. 2004 Apr;34(4):583-90.

Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined
by immunoglobulin E Western blotting, basophil-histamine release and
intracutaneous testing: Ara h2 is the most important peanut allergen.

Koppelman SJ(1), Wensing M, Ertmann M, Knulst AC, Knol EF.

15137814 J Agric Food Chem. 2004 May 19;52(10):2785-90.

Confirmation of the allergenic peanut protein, Ara h 1, in a model food matrix
using liquid chromatography/tandem mass spectrometry (LC/MS/MS).

Shefcheck KJ(1), Musser SM.

16968080 J Agric Food Chem. 2006 Sep 20;54(19):7180-6.

Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer.

van Boxtel EL(1), van Beers MM, Koppelman SJ, van den Broek LA, Gruppen H.

17031994 J Agric Food Chem. 2006 Oct 18;54(21):7953-9.

Confirmation of peanut protein using peptide markers in dark chocolate using
liquid chromatography-tandem mass spectrometry (LC-MS/MS).

Shefcheck KJ(1), Callahan JH, Musser SM.

17474754 J Agric Food Chem. 2007 May 30;55(11):4461-73. Epub 2007 May 3.

Proteomics-based approach to detect and identify major allergens in processed
peanuts by capillary LC-Q-TOF (MS/MS).

Chassaigne H(1), Nørgaard JV, Hengel AJ.

22364549 J Agric Food Chem. 2012 Mar 21;60(11):2934-42. doi: 10.1021/jf2052306. Epub 2012
Mar 9.

Digested Ara h 1 loses sensitizing capacity when separated into fractions.

Bøgh KL(1), Barkholt V, Rigby NM, Mills EN, Madsen CB.

22998620 J Agric Food Chem. 2012 Oct 17;60(41):10352-8. doi: 10.1021/jf302800e. Epub 2012
Oct 9.

Purification and characterization of Ara h1 and Ara h3 from four peanut market
types revealed higher order oligomeric structures.

Yusnawan E(1), Marquis CP, Lee NA.

25036339 Prep Biochem Biotechnol. 2015;45(5):438-46. doi: 10.1080/10826068.2014.940972.

Purification and recombinant expression of major peanut allergen Ara h 1.

Wu Z(1), Yan F, Wei X, Li X, Tong P, Yang A, Tang R, Chen H.

26471570 Food Chem. 2016 Mar 1;194:383-90. doi: 10.1016/j.foodchem.2015.08.024. Epub 2015
Aug 12.

Standardization of RP-HPLC methods for the detection of the major peanut
allergens Ara h 1, Ara h 2 and Ara h 3.

Singh H(1), Cantoria MJ(2), Malave P(2), Saputra D(3), Maleki S(4).

26921497 Food Chem Toxicol. 2016 May;91:82-90. doi: 10.1016/j.fct.2016.02.016. Epub 2016
Feb 26.

Allergenicity attributes of different peanut market types.

Koppelman SJ(1), Jayasena S(2), Luykx D(3), Schepens E(3), Apostolovic D(3), de
Jong GA(4), Isleib TG(5), Nordlee J(2), Baumert J(2), Taylor SL(2), Cheng H(6),
Maleki S(6).

28234343 Foods. 2014 Dec 18;3(4):642-657. doi: 10.3390/foods3040642.

Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding
to the Natural Protein.

Hurlburt BK(1), McBride JK(2), Nesbit JB(3), Ruan S(4), Maleki SJ(5).

30258615 Food Sci Nutr. 2018 Jul 27;6(6):1706-1714. doi: 10.1002/fsn3.742. eCollection
2018 Sep.

Effects of different thermal processing methods on the structure and
allergenicity of peanut allergen Ara h 1.

Tian Y(1)(2), Rao H(1)(2), Zhang K(1)(2), Tao S(3), Xue WT(1)(2).

31880850 Clin Exp Allergy. 2020 Mar;50(3):401-405. doi: 10.1111/cea.13554. Epub 2020 Feb

Identification of the amino-terminal fragment of Ara h 1 as a major target of the
IgE-binding activity in the basic peanut protein fraction.

Aalberse RC(1), Mueller GA(2), Derksen NIL(1), Aalberse JA(3), Edwards LL(2),
Pomés A(4), Lidholm J(5), Rispens T(1), Briza P(6).

33439436 Glycoconj J. 2021 Feb;38(1):67-76. doi: 10.1007/s10719-020-09969-1. Epub 2021 Jan

Purification and molecular characterization of a truncated-type Ara h 1, a major
peanut allergen: oligomer structure, antigenicity, and glycoform.

Md A(1), Maeda M(1), Matsui T(2), Takasato Y(2), Ito K(2), Kimura Y(3).