Ovalbumin | |||||||
---|---|---|---|---|---|---|---|
![]() | |||||||
Identifiers | |||||||
Organism | |||||||
Symbol | ? | ||||||
UniProt | P01012 | ||||||
|
Ovalbumin (abbreviated OVA [1]) is the main protein found in egg white, making up approximately 55% of the total protein. [2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. [3] The function of ovalbumin is unknown, although it is presumed to be a storage protein. [4]
Ovalbumin is an important protein in several different areas of research, including:
(For in vivo and in vitro studies based on ovalbumin it is important that the endotoxin content is less than 1 EU/mg.)[ citation needed][ needs context]
The ovalbumin protein of chickens consists of 385 amino acids, its relative molecular mass is 42.7 kDa, [5] and it adopts a serpin-like structure. [6] Ovalbumin also has several modifications, including N-terminal acetylation (G1), phosphorylation (S68, S344), and glycosylation (N292). [5] It has three isoforms, A1, A2, and A3, which vary based on the number of bound phosphate residues. [7] It is secreted from the cell, targeted by an internal signal sequence (residues 21–47), rather than the N-terminal signal sequence commonly found in other secreted proteins. Ovalbumin's signal sequence is not cleaved off, but remains as part of the mature protein. [8]
When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all- β-sheet structure with exposed hydrophobic regions. This causes the protein to aggregate and cause the solidification associated with cooked egg white. [9]
Ovalbumin | |||||||
---|---|---|---|---|---|---|---|
![]() | |||||||
Identifiers | |||||||
Organism | |||||||
Symbol | ? | ||||||
UniProt | P01012 | ||||||
|
Ovalbumin (abbreviated OVA [1]) is the main protein found in egg white, making up approximately 55% of the total protein. [2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. [3] The function of ovalbumin is unknown, although it is presumed to be a storage protein. [4]
Ovalbumin is an important protein in several different areas of research, including:
(For in vivo and in vitro studies based on ovalbumin it is important that the endotoxin content is less than 1 EU/mg.)[ citation needed][ needs context]
The ovalbumin protein of chickens consists of 385 amino acids, its relative molecular mass is 42.7 kDa, [5] and it adopts a serpin-like structure. [6] Ovalbumin also has several modifications, including N-terminal acetylation (G1), phosphorylation (S68, S344), and glycosylation (N292). [5] It has three isoforms, A1, A2, and A3, which vary based on the number of bound phosphate residues. [7] It is secreted from the cell, targeted by an internal signal sequence (residues 21–47), rather than the N-terminal signal sequence commonly found in other secreted proteins. Ovalbumin's signal sequence is not cleaved off, but remains as part of the mature protein. [8]
When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all- β-sheet structure with exposed hydrophobic regions. This causes the protein to aggregate and cause the solidification associated with cooked egg white. [9]