Isolation and characterization of sheep lactoferrin, an inhibitor of platelet aggregation and comparison with human lactoferrin

• Published in: Biochimica et biophysica acta 1995-01, Vol.1243 (1), p.25-32
• Main Authors: Qian, Zu-Yuan, Jollès, Pierre, Migliore-Samour, Danièle, Fiat, Anne-Marie
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; binding; blood platelets; comparisons; ewe milk; human-sheep lactoferrin interactions; Humans; interactions; Lactoferrin; Lactoferrin - chemistry; Lactoferrin - isolation & purification; Lactoferrin - metabolism; Lactoferrin - pharmacology; Milk; Milk - chemistry; Models, Molecular; Molecular Sequence Data; Peptide Fragments - chemistry; Platelet aggregation; Platelet Aggregation - drug effects; Platelet Aggregation Inhibitors - chemistry; Platelet Aggregation Inhibitors - isolation & purification; Platelet Aggregation Inhibitors - metabolism; Protein Binding; proteolysis; purification; sequence alignment; Sequence Analysis; Sequence Homology, Amino Acid; Sheep; Species Specificity
• ISSN: 0304-4165; 0006-3002; 1872-8006; 1878-2434
• DOI: 10.1016/0304-4165(94)00126-I

Highly purified sheep lactoferrin was isolated from ovine whey in a single chromatographic step (FPLC): it was characterized by electrophoresis, N-terminal sequence determination and compared with lactoferrins from other species. Sheep and human lactoferrins inhibited thrombin-induced platelet aggregation (median inhibitory concentration: IC 50 5 and 4 μM. respectively). Pepsin hydrolysates of human and sheep lactoferrins were fractionated by reverse-phase high-performance liquid chromatography and only one peak was an inhibitor of platelet aggregation. The sheep or human lactoferrin binding to platelets was studied.