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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