Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6; characterization of intermediate- and end products

2013 ◽  
Vol 1834 (12) ◽  
pp. 2832-2842 ◽  
Author(s):  
Danijela Apostolovic ◽  
Dion Luykx ◽  
Hans Warmenhoven ◽  
Dennis Verbart ◽  
Dragana Stanic-Vucinic ◽  
...  
Keyword(s):  
Peanut Allergen ◽  
Ara H 2 ◽  
End Products ◽  
Ara H 6

Characterization of the T-cell epitopes of a major peanut allergen, Ara h 2

Allergy ◽  
2005 ◽  
Vol 60 (1) ◽  
pp. 35-40 ◽  
Author(s):  
I. N. Glaspole ◽  
M. P. de Leon ◽  
J. M. Rolland ◽  
R. E. O'Hehir
Keyword(s):  
T Cell ◽  
T Cell Epitopes ◽  
Peanut Allergen ◽  
Ara H 2

High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2

2003 ◽  
Vol 31 (2) ◽  
pp. 250-259 ◽  
Author(s):  
Katrin Lehmann ◽  
Silke Hoffmann ◽  
Philipp Neudecker ◽  
Martin Suhr ◽  
Wolf-Meinhard Becker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Yield ◽  
Purification And Characterization ◽  
Peanut Allergen ◽  
Ara H 2 ◽  
Expression In Escherichia Coli

Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2

2005 ◽  
Vol 35 (4) ◽  
pp. 490-497 ◽  
Author(s):  
S. J. Koppelman ◽  
G. A. H. de Jong ◽  
M. Laaper-Ertmann ◽  
K. A. B. M. Peeters ◽  
A. C. Knulst ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Cross Reactivity ◽  
Peanut Allergen ◽  
Binding Properties ◽  
Ara H 2 ◽  
Ara H 6

scholarly journals Ara h 2 is the dominant peanut allergen despite similarities with Ara h 6

2020 ◽  
Vol 146 (3) ◽  
pp. 621-630.e5 ◽  
Author(s):  
Oliver Hemmings ◽  
George Du Toit ◽  
Suzana Radulovic ◽  
Gideon Lack ◽  
Alexandra F. Santos
Keyword(s):  
Peanut Allergen ◽  
Ara H 2 ◽  
Ara H 6

Characterization of the peanut allergen Ara h 6: Isolation and mapping of IgE-binding epitopes

2002 ◽  
Vol 109 (1) ◽  
pp. S286-S286
Author(s):  
Martin Suhr ◽  
Daniel Wicklein ◽  
Wolf Meinhard Becker
Keyword(s):  
Peanut Allergen ◽  
Ige Binding ◽  
Ara H 6

scholarly journals In Vitro Characterization of the Enzyme Properties of the Phospholipid N-Methyltransferase PmtA from Agrobacterium tumefaciens

2009 ◽  
Vol 191 (7) ◽  
pp. 2033-2041 ◽  
Author(s):  
Meriyem Aktas ◽  
Franz Narberhaus
Keyword(s):  
Agrobacterium Tumefaciens ◽  
In Vitro Assay ◽  
Enzyme Properties ◽  
Vitro Assay ◽  
Plant Infection ◽  
In Vitro Characterization ◽  
End Products ◽  
And Control

ABSTRACT Agrobacterium tumefaciens requires phosphatidylcholine (PC) in its membranes for plant infection. The phospholipid N-methyltransferase PmtA catalyzes all three transmethylation reactions of phosphatidylethanolamine (PE) to PC via the intermediates monomethylphosphatidylethanolamine (MMPE) and dimethylphosphatidylethanolamine (DMPE). The enzyme uses S-adenosylmethionine (SAM) as the methyl donor, converting it to S-adenosylhomocysteine (SAH). Little is known about the activity of bacterial Pmt enzymes, since PC biosynthesis in prokaryotes is rare. In this article, we present the purification and in vitro characterization of A. tumefaciens PmtA, which is a monomeric protein. It binds to PE, the intermediates MMPE and DMPE, the end product PC, and phosphatidylglycerol (PG) and phosphatidylinositol. Binding of the phospholipid substrates precedes binding of SAM. We used a coupled in vitro assay system to demonstrate the enzymatic activity of PmtA and to show that PmtA is inhibited by the end products PC and SAH and the antibiotic sinefungin. The presence of PG stimulates PmtA activity. Our study provides insights into the catalysis and control of a bacterial phospholipid N-methyltransferase.

589 Characterization of the major peanut allergen Ara h 1 on protein level

1996 ◽  
Vol 97 (1) ◽  
pp. 330-330
Author(s):  
W BECKER ◽  
L BUSCHMANN ◽  
M SCHLAAK
Keyword(s):  
Protein Level ◽  
Peanut Allergen ◽  
Ara H 1
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