Characterization of the protein and glycan moieties in different forms of bovine lactoferrin.
The BrCN cleavage of lactoferrin-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 30 kDas, or 74, 54, 47, and 30 kDas, respectively. N-Terminal amino acid sequence analyses show that the sequences of 58, 52, and 30 kDa fragments (residues 64-471, 130-471, and 472-689) of LF-a coincide with those of the 54, 47, and 30 kDa fragments of LF-b. respectively. All these fragments, which were positive by PAS staining, were not stained after being treated with glycopeptidase F. This treatment changed the 58 and 52 kDa fragments of LF-a to the 54 and 47 kDa fragments, respectively, whose molecular masses were the same as those of the treated fragments of LF-b. The 58 and 52 kDa fragments of LF-a bound to the lectin, Ricinus communis agglutinin, while the 54 and 47 kDa fragments of LF-b hardly bound to it.
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Faculty of Applied Biological Science, Hiroshima University, Japan.
Nishimura
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Yoshida
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D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D006031:Glycosylation; D007781:Lactoferrin / Q000737:chemistry*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D010446:Peptide Fragments; D011134:Polysaccharides; D007781:Lactoferrin; D003488:Cyanogen Bromide