Abstract
Summary Properties of three equine milk proteins, lysozyme, α‐lactalbumin, and β‐lactoglobulin, were investigated and compared with the corresponding ones of bovine milk. The subsite structure similar to that in hen egg lysozyme was assumed in the functional region of lysozyme from interaction with inhibitors. α‐lactalbumin has structures similar to those of bovine, but less stability of its intact and 3SS forms are observed than the corresponding bovine irrespective of [Ca2+] because of the entropy factors. Although the folding of β‐lactoglobulin at acid pH is very similar to that of the bovine protein the conformation of the I strand is different from that of bovine I strand at neutral pH according to NMR data.
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