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LF f(267-288) [id=LFB0148]

Producer Organism : Native Protein : Production Method :
Cow 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.

Likely antimicrobial but not tested pure.
Length : 22 Mass (Da): 2 637.79 Common Amino Acids : K
Isolectric Point : 11.37 Net Charge : 5 Absent Amino Acids : CDHMPTVY
Basic Residues : 6 Acidic Residues : 1 Hydrophobic Residues : 8
Polar Residues : 5 Boman Index : -46.68 Hydropathy Index : -0.836
Aliphatic Index : 75.45 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 261.9

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)


 1 LFBNATIVE 100.0%    SVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQR   
 2 LFB0133    95.0%    ------GLIWKLLSKAQEKFGKNKSR------------   
 3 LFB0146   100.0%    -------LIWKLLSKAQEKFGKNKSR------------   
 4 LFB0128   100.0%    ------DLIWKLLSKAQEKF------------------   
 5 LFB0141    95.0%    ------DLIWKLLSKAQEKFGGNKSR------------   
 6 LFB0129   100.0%    ------DLIWKLLSKAQEKFGK----------------   
 7 LFB0142    95.0%    ------DLIWKLLSKAQEKFGKNGSR------------   
 8 LFB0130   100.0%    ------DLIWKLLSKAQEKFGKNK--------------   
 9 LFB0143    95.0%    ------DLIWKLLSKAQEKFGKNKSG------------   

10 LFB0123   100.0%    SVDGKEDLIWKLLSKAQEKFGKNKSR------------   

11 LFB0125   100.0%    --DGKEDLIWKLLSKAQEKFGKNKSR------------   

12 LFB0126   100.0%    ----KEDLIWKLLSKAQEKFGKNKSR------------   

13 LFB0140    95.0%    ------DLIWKLLSKAQEGFGKNKSR------------   

14 LFB0139    95.0%    ------DLIWKLLSKAQGKFGKNKSR------------   

15 LFB0138    95.0%    ------DLIWKLLSGAQEKFGKNKSR------------   

16 LFB0127   100.0%    -----EDLIWKLLSKAQEKFGKNKSR------------   

17 LFB0135    95.0%    ------DLGWKLLSKAQEKFGKNKSR------------   

18 LFB0150   100.0%    -----------LLSKAQEKFGKNKSR------------   

19 LFB0136    95.0%    ------DLIGKLLSKAQEKFGKNKSR------------   

20 LFB0137    95.0%    ------DLIWGLLSKAQEKFGKNKSR------------   

21 LFB0131   100.0%    ------DLIWKLLSKAQEKFGKNKSR------------   

22 LFB0134    95.0%    ------DGIWKLLSKAQEKFGKNKSR------------   

23 LFB0149   100.0%    ---------WKLLSKAQEKFGKNKSR------------   

24 LFB0147   100.0%    --------IWKLLSKAQEKFGKNKSRS-----------   

25 LFB0148   100.0%    --------IWKLLSKAQEKFGKNKSRSFQL--------   

26 LFB0151   100.0%    ------------------KFGKNKSRSFQL--------   
27 LFB0144   100.0%    ------DLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQR   

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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