Amino terminal sequence, processing, and biological activity of porcine pre-alpha-lactalbumin.

Polyadenylated RNAs isolated from bound polysomes of a lactating sow's mammary gland, were translated in a cell-free system and in vitro synthesized alpha-lactalbumin was immunoprecipitated and radiosequenced. The translation product was found to contain an amino terminal extension of 19 amino acid residues, very similar to its ovine counterpart, that was selectively removed when translation was carried out in the presence of rabbit mammary microsomal membranes. Assays of porcine pre-alpha-lactalbumin for activity on galactosyltransferase showed that the preprotein can also interact with and modify the specificity of the enzyme, as indicated by de novo synthesis of lactose.