title: Mode of interaction between lysozyme and the other proteins of the hen's egg vitelline membrane.
abstract: Salt solutions and charged detergents are efficient solubilizing agents for ovovitelline membrane lysozyme. Reassociation experiments with chemically modified lysozymes indicate that positively charged amino acid residues of lysozyme (the epsilon-amino group of lysine and the guanidino group of arginine) are involved in the interaction with other proteins of the vitelline membrane. Exogenous proteins are adsorbed to lysozyme-free vitelline membranes, only if they have a high pI, comparable to that of lysozyme. It is concluded that the lysozyme-ovovitelline membrane interaction is predominantly ionic. An ovomucin-lysozyme complex is postulated as the major component of the outer layer of the membrane.
mesh_terms: D000818:Animals; D002645:Chickens; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000302:isolation & purification / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D014817:Vitelline Membrane / Q000378:metabolism*
chemical_list: D011506:Proteins; D009113:Muramidase