. Beta- lactoglobulin is the major whey protein in the milk of ruminants and some nonruminants. It was first isolated 60 years ago and a wealth of physico-chemical and biological information has been accumulated.
The amino acid sequences have been determined for b-lactoglobulins of several species and several DNA sequences and gene structures have been reported. The conformational structure of b-lactoglobulin has been studied by x-ray crystallography. The core of the molecule is made up of a very short a-helix segment and eight strands of anti-parallel b-sheet, which wrap round to form an antiparallel b-barrel. An interesting physico-chemical property of b-lactoglobulin is its ability to bind in vitro small hydrophobic substances such us retinol and fatty acids.

Comments and contributions are welcomed

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