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LF f(17-31) [id=LFS0001]

Producer Organism : Native Protein : Production Method :
Sheep Lactoferrin (LF) Enzymatic hydrolysis and Purification with LC method
Activity : Not determined
Target Organisms :

Unavailable data

Description :
Production method: Pepsin hydrolysis and purification with LC method.

The sequence 17-31 of sheep lactoferrin is more hydrophilic than the bovine one. It would be interesting to know if this sequence of sheep lactoferrin would enhance the bactericidal activity observed with the bovine analogous peptide (Citation: 1).
Length : 33 Mass (Da): 3 914.43 Common Amino Acids : K
Isolectric Point : 11.31 Net Charge : 8 Absent Amino Acids : DFHT
Basic Residues : 9 Acidic Residues : 1 Hydrophobic Residues : 8
Polar Residues : 8 Boman Index : -85.03 Hydropathy Index : -1.109
Aliphatic Index : 50.3 Instability Index : 0 Extinction Coefficient : 12615
Absorbance 280nm : 394.22

Wheel representation

Hydrophobicity plot

Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Citation: 1

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

Cited Entries: LFS0001

Authors:Qian, Z.-Y., Jolles, P., Migliore-Samour, D., Fiat, A.-M.
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects 1995, 1243(1).
CrossRef External Link
Abstract: 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: IC50 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.
Keywords: Lactoferrin; Platelet aggregation; Milk; Sheep

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