6.2.1 Molecular Biological Properties
 

Lipid-transfer Protein	References
Allergen Nomenclature Pru p 3	(1) Larsen & Lowenstein 2000
Molecular Mass  SDS-PAGE: 13 kDa (2), 9 kDa (1) MALDI-MS: 9138 Da (2)	(1) Pastorello et al. 1999 (2) Sánchez-Monge et al. 1999
Isoelectric Point  calculated: pI 9.25 (1) IEF-PAGE: pI > 9 kDa (1)	(1) Pastorello et al. 1999
Amino Acid Sequence, RNA, and cDNA Pru p 3 (1) SWISS-PROT: P81402 GenBank: GI:3287877 Amino Acids 91 aa mRNA   cDNA   N-terminus: aa 1-22 (2): ITXGQVSSSLAPXIPYVRGGGA	(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 Lipid-transfer protein from apricot: 94% aa identity to N-terminal sequence (3) Lipid-transfer protein from apple: 86% aa identity to N-terminal sequence (2) Lipid-transfer proteins from rice, maize, tomato, and spinach: average 65% aa identity to N-terminus (1)	(1) Pastorello et al. 1999 (2) Sánchez-Monge et al. 1999 (3) Pastorello et al. 2000

 6.2.2 Allergenic Properties
 

Lipid-transfer Protein	References
Frequency of Sensitization IgE-binding to Pru p 3 in 86% to 100% of patients (1)	(1) see 6.1 Sensitization to Peach Allergens