Ovotransferrin Antibody, FITC conjugated

1. unfolding pathway and conformational stability of conalbumin PMID: 21833676
2. glycosylation of fetal & hen ovotransferrin differs; hypothesized to alter ovotransferrin recognition by carbohydrate binding lectins PMID: 7881176
3. studied the carbohydrate and amino acid compositions of the ovotransferrin glycopeptides PMID: 574451
4. The exon structure of the ovotransferrin gene confirms the duplication event to produce two homologous domains that make up ovotransferrin PMID: 3658709
5. evidence suggests that conalbumin (ovotransferrin) and transferrin are products of the same gene, differing only in carbohydrate content PMID: 4907959
6. show both lobes are required for efficient iron binding and calculate binding kinetics. PMID: 6319414
7. ovotransferrin folds into two compact, iron-binding domains; the authors demonstrate that the duplicated domain structure is necessary to retain ovotransferrin in plasma and stop immediate loss via kidney filtration PMID: 6805466
8. The structure of ovotransferrin shows that the iron-binding site is located in the interdomain cleft in each lobe; differences in ovotransferrin structure cause changes to iron binding & uptake/release compared to lactotransferrin & transferrin. PMID: 7490743
9. At a pH where the protein net charge is negative (pH 8.0), the behavior of ovotransferrin at the air-water interface is more influenced by charge effects rather than bulk concentration effects. PMID: 21316692
10. Trp-Asn-Ile-Pro and Gly-Trp-Asn-Ile peptides of ovotransferrin showed the highest antioxidant activity. PMID: 20568771
11. Marked stabilization effects by amino(N)- and carboxyl(C)-terminal lobes of ovotransferrin are induced during iron binding, primarily upon N-lobe iron binding in the iron-free C-lobe and secondarily upon C-lobe iron binding in the monoferric N-lobe. PMID: 15323571
12. Ovotransferrin is able to cleave itself through the unique chemical reactivity of four tripeptides motifs, HTT (residues 209-211), HST (residues 542-544) and two CHT (residues 115-117 and 454-456). PMID: 16442235
13. Several proteins associated with the egg shell membranes (ESM) with antibacterial activity have been identified including ovotransferrin, in addition, pure fractions of ovotransferrin were obtained from egg white. PMID: 16721662

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KEGG: gga:396241

UniGene: Gga.2551