Saposin-C from bovine spleen; complete amino acid sequence and relation between the structure and its biological activity.

Saposin-C, a small acidic glycoprotein that can activate glucosylceramide-beta-glucosidase, has been isolated from bovine spleen. The complete amino acid sequence of bovine saposin-C was determined by Edman degradation of the purified protein and its fragmented peptides. It contains 80 amino acids, one carbohydrate chain attached to a single asparagine residue and six cysteine residues in oxidized form. The sequence of bovine saposin-C is 76 and 65% identical with the sequences of saposin-C from human spleen and guinea pig liver, respectively. Hydropathy profiles of the sequence of saposin-C from three species were similar despite the significant residue substitutions. Bovine saposin-C had a stronger effect in stimulating bovine beta-glucosidase compared to human saposin-C. However, the effect of human saposin-C in stimulating human enzyme was stronger than that of bovine saposin-C. The region around residue 35, which is next to the extremely hydrophilic region, seems to be important to produce an interaction with the enzyme.