Purification of goats’ milk casein by reversed-phase high-performance liquid chromatography and identification of αsl-casein

Goats‘ milk caseins were separated into four components in a single run using reversed-phase gradient high-performance liquid chromatography. The purity of the isolated components was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis, amino acid analysis and determination of the N-terminal residue. By a comparison with previously published results for goats’ milk caseins the four peaks were identified as k-, sl-, as2- and /?-casein. In order to confirm the existence of αsl-casein in goats' milk, this component was sequenced for 44 steps, revealing a sequence homologous to bovine αsl-casein and almost identical to the N-terminal sequence previously published by Boulanger et al. (1984).