Disulfide-linked homodimer. A tetramer is also observed at neutral pH.
Allergen epitopes:
Not known
Allergen stability: Process, chemical, enzymatic
Not known
Nature of main cross-reacting proteins:
Not known
Allergen properties & biological function:
Protein component of the very low density lipoprotein found in egg yoke. A potent lipoprotein lipase inhibitor, preventing the loss of triglycerides. As the quail homologue has no intermolecular disulphide, this may not be required for function.
Allergen purification:
George et al. (1987) [1243] and Nimpf et al. (1988) [1535] report a purification of very low density lipoprotein II (apovitellenin I).
Other biochemical information:
Homologous proteins from other birds (quail, turkey and duck) have more than 70% sequence identity and IgE cross-reactivity is likely.
References (4)
George R, Barber DL, Schneider WJ.
Characterization of the chicken oocyte receptor for low and very low density lipoproteins.
J Biol Chem. 262(35):16838-16847.
1987
PUBMED ID:
3119592
MacLachlan I, Steyrer E, Hermetter A, Nimpf J, Schneider WJ.
Molecular characterization of quail apolipoprotein very-low-density lipoprotein II: disulphide-bond-mediated dimerization is not essential for inhibition of lipoprotein lipase.
Biochem J. 317 ( Pt 2):599-604. 1996
PUBMED ID:
8713091
Nimpf J, George R, Schneider WJ.
Apolipoprotein specificity of the chicken oocyte receptor for low and very low density lipoproteins: lack of recognition of apolipoprotein VLDL-II.
J Lipid Res. 29(5):657-667. 1988
PUBMED ID:
3411240
Walsh BJ, Barnett D, Burley RW, Elliott C, Hill DJ, Howden ME.
New allergens from hen's egg white and egg yolk. In vitro study of ovomucin, apovitellenin I and VI, and phosvitin.
Int Arch Allergy Appl Immunol. 87(1):81-86. 1988
PUBMED ID:
3170012