Characterization of the Protein and Glycan Lactoferrin Moieties in Different Forms of Boyine

The BrCN cleavage of lacteferrin-a or -b (LF-a or LF-b) led to the observation of four fragments by SDS-PAGE, whose molecular masses were 77, 58, 52, and 30kDas, or 74, 54, 47, and 30 kDas, respectiyely. N-TeTmina} amino acEd sequence analyses show that the sequences of 58, 52, and 30 kDa fragments (residues 6"71, 130-471, and 472-689) of LF-a coincide vvith those of the 54, 47, anG 30kDa fragments of LF-b, respectiyely, . All these fragments, which were positive by PAS staining, were not stained after being treated with glycopeptidase F. This treatment ehanged the 58 and 52 kDa frngments of LF-a to the 54 and 47 kDa fragments, respectiyely, whose molecular masses were the same as those of the treated fragments of LF-b. The 58 and 52kDa t"ragments of LF-a bound to the lectin, Ricinus communis agglutinin, while the 54 and 47 kDa t'ragments of LF-b hardly bound to it.