Avidin

Literature References: Basic glycoprotein isolated from raw egg white. Exhibits high binding affinity for biotin and is capable of producing biotin deficiency in rats and chicks. Occurs in the white portion of eggs and the oviducts of birds and amphibia. Destroyed by cooking or irradiation. Isoln: Eakin et al., J. Biol. Chem. 136, 801 (1940); Pennington et al., J. Am. Chem. Soc. 64, 469 (1942); Fraenkel-Conrat et al., Arch. Biochem. Biophys. 39, 80, 97 (1952). Improved purification and crystallization: Green et al., Biochem. J. 118, 67, 71 (1970). Structure is a glycoprotein containing four essentially identical subunits: Green, ibid. 92, 16c (1964). The combined mol wt of the subunits is about 66,000. Each subunit is a single polypeptide chain containing 128 amino acid residues with alanine at the N-terminal, glutamic acid at the C-terminal, and a carbohydrate moiety attached at the asparaginyl residue, position 17. Complete amino acid sequence of the protein subunit: DeLange, Huang, J. Biol. Chem. 246, 698 (1971). Studies on biotin inactivation by avidin: Becker, Wilchek, Biochim. Biophys. Acta 264, 165 (1972). Review of chemistry and binding properties: N. M. Green, Adv. Protein Chem. 29, 85-133 (1975). Review of use of avidin-biotin complex in molecular biology: E. A. Bayer, M. Wilchek, Methods Biochem. Anal. 26, 1-45 (1980); in immunoassays: M. Wilchek, E. A. Bayer, Immunol. Today 5, 39-43 (1984).