4.4.1 Molecularbiological Properties
 

Ovotransferrin (OT)	References
Allergen Nomenclature  Gal d 3	(1) King et al. 1994
Molecular Mass Mr 77.3-77.7 kDa  4 isoforms by mass spectrometry (1)	(1) Awade et al. 1994
Isoelectric Point  pI 5.6 - 6.2 (1)  iron-free form: pI 7.17, monoferric form: pI 6.68, 2 Fe/mol OT: pI 6.24 and pI 6.09 (cIEF) (2)	(1) Holen & Elsayed 1990  (2) Richards & Huang 1997
Amino Acid Sequence  SWISS-PROT: P01012  686 residues (1)	(1) Williams et al. 1982
cDNA Sequence  EMBL:  J00895	(1) Cochet et al. 1979  (2) Jeltsch et al. 1987
mRNA Sequence  nucleotides (1), Sequence (1)	(1) Jeltsch & Chambon 1982
recombinant OT  expression in baby hamster kidney cells (1)	(1) Mason et al. 1996
3D-Structure  monoferric N-terminal half-molecule (1)	(1) Dewan et al. 1993
Posttranslational Modifications  Disulfide bonds:  12 disulfide bonds: 10-45, 115-197, 160-174, 171-182, 228-242, 348-380, 405-680, 421-643, 454-530, 478-671, 488-502, 499-513 (2) additional bonds: 20-36 / 358-371 / 570-584 (2)  Glycosylation of OT:  carbohydrate content: 2.6% of whole Mr (1)  carbohydrate composition: 1.7% GlcNAc, 0.9% Man (1)  1 N-glycosylation site: 473  structures of glycans (mass spectrometry) (3)  biantennary glycans (hydrazinolysis, methanolysis, methylation analysis and, 1H-NMR spectroscopy) (4)	(1) Robinson 1972  (2) Williams et al. 1982  (3) Yet et al. 1990  (4) Jacquinot et al. 1994
Genetic Variants  replacement of residues: 64 (A/V), 81 (V/I), 135 (R/W), 220-221 (Q/K-L/N), 667 (S/N) (1)	(1) SWISS-PROT: P01012
Biological Function  iron transport:   domain I 1-332   domain II 342-686   active sites: iron binding 60 / 92, 191 / 250, 395 / 431, 524 / 592, anion bindung: 121 / 460 (1)  antimicrobial activity (2)	(1) SWISS-PROT: P01012  (2) Valenti et al. 1983

 

4.4.2 Allergenic Properties
 

Ovotransferrin (OT)	References
Immunoglobulines  IgE-binding studies (1)	(1) see 4.1 Sensitization to Egg White Allergens