The Amino Acid Sequence of Goatß-Lactoglobulin

Abstract

The isolation of .beta.-lactoglobulin from milk of the goat is described. The purified protein was checked for purity and was characterized by its gross composition and end groups. The native or the modified protein was then degraded by tryptic and cyanogen bromide cleavage. The cleavage products were isolated and sequenced in the sequenator using a Quadrol and propyne program. These data provide the complete sequence of .beta.-lactoglobulin of the goat. The results are discussed and compared particularly with bovine .beta.-lactoglobulin components AB. Some biological aspects are described.