LF f(14-42) [id=LAG0001]

Producer Organism : Native Protein : Production Method :
Goat Lactoferrin (LF) Enzymatic hydrolysis and Purification with LC method
Activity : Antibacterial
Target Organisms :

Gram-positive: Micrococcus flavus DSM 1790 (MIC=7 ÁM).

Gram-negative: Escherichia coli ATCC 25922 (MIC=56 ÁM).

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

Length : 29 Mass (Da): 3 496.80 Common Amino Acids : R
Isolectric Point : 11.45 Net Charge : 6 Absent Amino Acids : DFHN
Basic Residues : 7 Acidic Residues : 1 Hydrophobic Residues : 7
Polar Residues : 9 Boman Index : -91.06 Hydropathy Index : -0.976
Aliphatic Index : 43.79 Instability Index : 0 Extinction Coefficient : 12615
Absorbance 280nm : 450.54

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.

Multiple Sequence Alignment (MSA)

 3 LAG0011  93.8%  ------YQWQRRMR-LGAPSIT------- 
 4 LAG0012 100.0%  --------WQRRMRKLGAPSIT------- 
 5 LAG0013  92.9%  --------WQRRM-KLGAPSIT------- 
 6 LAG0010  93.8%  ------YQWQRRM-KLGAPSIT------- 
 7 LAG0008 100.0%  ------YQWQRRMRKLGAPSIT------- 
 8 LAG0009  93.8%  ------YQWQR-MRKLGAPSIT------- 


11 LAG0002 100.0%  ---SKCYQWQRRMRKLGA----------- 
12 LAG0003  93.3%  ---SKCYQWQWRMRKLGA----------- 

13 LAG0007 100.0%  ------YQWQRRMRKL------------- 

Citation: 1

Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: a comparative study

Cited Entries: LFB0085, LFB0092, LAG0001, LAG0014

Authors:Recio, I., Visser, S.
Journal: International Dairy Journal 2000, 10(9).
CrossRef External Link
Abstract: A cation-exchange chromatographic membrane was used for the rapid isolation of caprine and ovine lactoferrin (LF) from cheese whey. Caprine LF was isolated by one-step cation-exchange chromatography, but the isolation of ovine LF needed a further reversed-phase HPLC purification step. The antibacterial activity of these LFs, determined towards Micrococcus flavus and Escherichia coli, was compared with that of bovine LF. Of the apo-LFs the caprine protein had the highest activity. In all cases the holo-LFs showed low or negligible activity. The antibacterial properties of cationic peptides obtained by peptic hydrolysis of caprine LF were studied against E. coli and M. flavus, and the activity of these peptides was compared with that of bovine lactoferricin. In addition, the binding characteristics of bovine, ovine and caprine LF to bacterial cells of E. coli were investigated with an enzyme-linked binding assay using horseradish peroxidase-bovine LF as a conjugate. Ovine and bovine LF strongly inhibited the binding of the LF complex to the bacterial surface. The iron-free forms of these LFs showed a greater ability for binding to the bacterial cells than the iron-saturated forms. However, several cationic peptides and caprine LF did not inhibit the binding of the LF conjugate although they exhibited a marked antibacterial effect. The results of binding of the LF complex in the presence of LFs from different species and of membrane-active peptides are discussed in relation to the antibacterial activity of these proteins and peptides.
Keywords: Lactoferrin; bovine; Ovine; Caprine; Antibacterial peptides; Antibacterial activity; Bacterial cell binding

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