Allergen Data Collection - Update: Apple (Malus domestica)
Internet Symposium on Food Allergens 2(Suppl.4): 1-23  (2000) [http://www.food-allergens.de]
6.4 Properties of Lipid-transfer Protein (Mal d 3)

6.4.1 Molecular Biological Properties
 
Lipid-transfer Protein References
Allergen Nomenclature Mal d 3 (1) Larsen & Lowenstein 1999
Molecular Mass 
SDS-PAGE: 13 kDa (2), 9 kDa (1)
MALDI-MS: 9058 Da (2)
(1) Pastorello et al. 1999
(2) Sánchez-Monge et al. 1999
Isoelectric Point pI 7.5 (IEF-PAGE)
(1) Pastorello et al. 1999
Amino Acid Sequence
N-terminus:
aa 1-31 (2): ITXGQVTSSLAPXIGYVRSGGAVPPAXXNGI
aa 1-36 (1): ITCGQVTSSLAPCIGYVRSGGAVPPACCNGIRNING
(1) Pastorello et al. 1999
(2) Sánchez-Monge et al. 1999
Posttranslational Modifications
Glycosylation:
no detection of carbohydrate moieties in SDS-PAGE with periodic acid- Schiff staining (1)
(1) Pastorello et al. 1999
Biological Function
Lipid-transfer proteins are involved in plant defense mechanisms and probably participate in formation of extracellular lipophilic substances (cutin, wax) (1)
(1) Sánchez-Monge et al. 1999
Sequence Homology
N-terminus of lipid-transfer proteins from almond, peach, and grape: 87%, 86%, and 61% identity to N-terminal sequence (1)
N-terminus of pollen allergens from Parietaria judaica (Par j 1.0102) and Brassica rapa: 32% and 23% identity to N-terminal sequence (1)
(1) Sánchez-Monge et al. 1999

 6.4.2 Allergenic Properties
 
Lipid-transfer Protein References
Frequency of Sensitization
IgE-binding to Mal d 3 in 28-100% of patients (1)
(1) see 6.1 Sensitization to Apple Allergens

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