LF f((1-16) - (45-48)) [id=LFB0010]

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

Gram-positive: Micrococcus flavus DSM 1790 (no MIC).

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

Length : 21 Mass (Da): 2 415.20 Common Amino Acids : R
Isolectric Point : 9.91 Net Charge : 3 Absent Amino Acids : DFGHLMY
Basic Residues : 4 Acidic Residues : 1 Hydrophobic Residues : 7
Polar Residues : 5 Boman Index : -50.55 Hydropathy Index : -0.6
Aliphatic Index : 60.48 Instability Index : 0 Extinction Coefficient : 11125
Absorbance 280nm : 556.25

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

Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin: In situ enzymatic hydrolysis on an ion-exchange membrane

Cited Entries: LFB0006, LFB0010, LFB0085, LFB0092, LFB0147, LFB0148, LFB0151, CAA0013, CAA0019, CAA0020

Authors:Recio, I., Visser, S.
Journal: Journal of Chromatography A 1999, 831(2).
CrossRef External Link
Abstract: Two ion-exchange chromatographic methods are reported for the rapid isolation of antibacterial peptides from lactoferrin (LF). Using the first method, a pepsin hydrolysate of LF was fractionated by bead-based cation-exchange chromatography. After removal of weakly bound material by washing with ammonia, highly purified lactoferricin-B (LFcin-B) was obtained in a single step by elution with 2 M NaCl. Some other cationic peptides, copurified as minor components, were also characterised by N-terminal sequencing, mass spectrometry and antibacterial activity determination. With the second method, cheese whey was filtered through a cation-exchange membrane, and the selectively bound LF was directly hydrolysed in situ with pepsin. Inactive LF fragments were washed off the membrane with ammonia, and a fraction enriched in LFcin-B was obtained by further elution with 2 M NaCl. The membrane method is more rapid and offers several economic advantages.
Keywords: peptides; ANTIBACTERIAL agents; Lactoferrin

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