Abstract
The interaction between ovomucin and egg white proteins has been investigated. Ovomucin interacted not only with lysozyme but also with such proteins in egg white as ovalbumin and conalbumin. The interaction increased correspondingly as the lysine content of proteins become higher. The maximum turbidity of ovomucin-lysozyme aggregates was proportionally dependent on the rate of acetylation of lysozyme, but that of ovomucin-ovalbumin aggregates was slightly dependent on the rate of acetylation of ovalbumin. The ovomucin-protein interaction decreased remarkably by the removal of sialic acid in ovomucin, but increased by the removal of polyhydroxyl group in sialic acid. From these results, the binding site of interaction was considered in detail. © 1976, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
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CITATION STYLE
Kato, A., Yoshida, K., Matsudomi, N., & Kobayashi, K. (1976). The Interaction between Ovomucin and Egg White Proteins. Agricultural and Biological Chemistry, 40(12), 2361–2366. https://doi.org/10.1271/bbb1961.40.2361
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