Hen egg white ovomacroglobulin has a protease inhibitory activity.
Hen egg white ovomacroglobulin purified by Miller and Feeney without reference to its activity was shown to have a protease inhibitory activity towards trypsin, papain, and thermolysin. It has four subunits of equal molecular weight (175,000 by SDS-PAGE) and each two of which are disulfide bonded. Upon incubation with trypsin it yields a fragment of Mr = 80,000 plus smaller ones. The subunit composition, amino acid composition and a newly found protease inhibitory activity place ovomacroglobulin as a closely related protein to human serum alpha 2-macroglobulin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D004529:Egg White; D005260:Female; D006801:Humans; D008259:Macroglobulins / Q000494:pharmacology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010206:Papain / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors / Q000494:pharmacology*; D013820:Thermolysin / Q000037:antagonists & inhibitors; D014357:Trypsin / Q000378:metabolism; D000511:alpha-Macroglobulins
D000596:Amino Acids; D008259:Macroglobulins; D046911:Macromolecular Substances; D011480:Protease Inhibitors; D000511:alpha-Macroglobulins; C036828:ovomacroglobulin; D014357:Trypsin; D010206:Papain; D013820:Thermolysin