High impact information on OVOS

• A stretch of 34 amino acid residues of the ovostatin bait region sequence was determined and the matrix metalloproteinase cleavage sites identified [1].
• Thus, proteinase-bound ovostatin has a uniform structure with a 2-fold axis of symmetry [2].
• Both free and thermolysin-bound ovostatin preparations were negatively stained with uranyl acetate, a series of three pictures were taken at 10 degrees specimen tilt intervals (+10 degrees, 0 degrees, and -10 degrees), and images of the inhibitor molecules were observed in three dimensions [2].
• The results support the unique mechanism of inhibition of proteinases by alpha 2-macroglobulin and ovostatin postulated from biochemical observations (Barrett, A. J., and Starkey, P. M. (1973) Biochem. J. 133, 709-724; Nagase, H., and Harris, E. D., Jr. (1983) J. Biol. Chem. 258, 7490-7498) [2].
• 9. The protease activity is inhibited by chelators, Z-phenylalanine, ovostatin, and tissue inhibitor of metalloproteinase from human articular cartilage [3].

Biological context of OVOS

• Ovostatin: a novel proteinase inhibitor from chicken egg white. I. Purification, physicochemical properties, and tissue distribution of ovostatin [4].
• Amino acid sequence of a 32-residue region around the thiol ester site in duck ovostatin [5].

Associations of OVOS with chemical compounds

• The results indicate that ovostatin is a close relative to plasma alpha-macroglobulins and may share a common ancestor with C3 and C4 [5].
• The Cys-to-Asn substitution forms the chemical basis for the lack of thiol esters in hen egg-white ovostatin [6].

Other interactions of OVOS

• From these electron microscopic studies we propose that a proteinase reaches to the center of the free ovostatin molecule and attacks the bait region [2].

Analytical, diagnostic and therapeutic context of OVOS

• Conformational changes of duck ovostatin (ovomacroglobulin) upon complexing with thermolysin have been studied by electron microscopy [2].
• The complete amino acid sequence of the hen ovomacroglobulin (ovostatin) subunit has been determined from cDNA and partial peptide sequence analysis [7].

References