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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2015.08.008
|2 doi
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|a pubmed24n0841.xml
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|a (DE-627)NLM252311361
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|a (NLM)26322854
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|a (PII)S0981-9428(15)30088-7
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Wilson, Karl A
|e verfasserin
|4 aut
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| 245 |
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|a Proteolysis of the peanut allergen Ara h 1 by an endogenous aspartic protease
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 02.09.2016
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2015 Elsevier Masson SAS. All rights reserved.
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|a The 7S and 11S globulins of peanuts are subjected to proteolysis two days after seed imbibition, with Ara h 1 and the arachin acidic chains being among the first storage proteins to be mobilized. Proteolytic activity was greatest at pH 2.6-3 and is inhibited by pepstatin A, characteristic of an aspartic protease. This activity persists in seedling cotyledons up to at least 8 days after imbibition. In vitro proteolysis of Ara h 1 at pH 2.6 by extracts of cotyledons from seedlings harvested 24 h after seed imbibition generates newly appearing bands on SDS-PAGE. Partial sequences of Ara h 1 that were obtained through LC-MS/MS analysis of in-gel trypsin digests of those bands, combined with information on fragment size, suggest that proteolysis begins in the region that links the two cupin domains to produce two 33/34 kD fragments, each one encompassing an intact cupin domain. The later appearance of two 18 and 10/11 kD fragments can be explained by proteolysis within an exposed site in the cupin domains of each of the 33/34 kD fragments. The same or similar proteolytic activity was observed in developing seeds, but Ara h 1 remains intact through seed maturation. This is partly explained by the observation that acidification of the protein storage vacuoles, demonstrated by vacuolar accumulation of acridine orange that was dissipated by a membrane-permeable base, occurs only after germination. These findings suggest a method for use of the seed aspartic protease in reducing peanut allergy due to Ara h 1
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a 7S globulin storage protein
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|a Allergen
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|a Ara h 1
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|a Aspartic protease
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|a Germination
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|a Peanut
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|a Proteolysis
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| 650 |
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|a Antigens, Plant
|2 NLM
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| 650 |
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|a Ara h 1 protein, Arachis hypogaea
|2 NLM
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| 650 |
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|a Glycoproteins
|2 NLM
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| 650 |
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|a Membrane Proteins
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Aspartic Acid Proteases
|2 NLM
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| 650 |
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|a EC 3.4.-
|2 NLM
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| 700 |
1 |
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|a Tan-Wilson, Anna
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 96(2015) vom: 27. Nov., Seite 301-10
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
1 |
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|g volume:96
|g year:2015
|g day:27
|g month:11
|g pages:301-10
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|u http://dx.doi.org/10.1016/j.plaphy.2015.08.008
|3 Volltext
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|d 96
|j 2015
|b 27
|c 11
|h 301-10
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