De Boeck S, Stockx J
Int J Biochem. 1986;18(7):623-8. doi: 10.1016/0020-711x(86)90292-2.
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.
盐溶液和带电荷的去污剂是卵黄膜溶菌酶的有效增溶剂。用化学修饰的溶菌酶进行的重缔合实验表明，溶菌酶带正电荷的氨基酸残基（赖氨酸的ε-氨基和精氨酸的胍基）参与了与卵黄膜其他蛋白质的相互作用。只有当外源蛋白质的pI值与溶菌酶的pI值相近时，它们才会吸附到不含溶菌酶的卵黄膜上。由此得出结论，溶菌酶与卵黄膜的相互作用主要是离子性的。推测卵黏蛋白-溶菌酶复合物是膜外层的主要成分。
