PMID:7980873
| Citation |
Loleit, M, Deres, K, Wiesmüller, KH, Jung, G, Eckert, M and Bessler, WG (1994) Biological activity of the Escherichia coli lipoprotein: detection of novel lymphocyte activating peptide segments of the molecule and their conformational characterization. Biol. Chem. Hoppe-Seyler 375:407-12 |
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| Abstract |
The lipoprotein (LP) from Escherichia coli and other Enterobacteriaceae as well as lipoprotein derived lipopeptides constitute potent B lymphocyte mitogens. Several synthetic peptide segments of the lipoprotein were tested for mitogenic activity towards splenocytes of BALB/c mice. Mitogenic effects were observed for the lipoprotein fragments LP-(2-15), LP-(2-20), LP-(2-25), and LP-(33-47), and a less pronounced effect was determined for LP-(2-10). The mitogenicity of the peptides could be further enhanced by their attachment to the lipopeptide N-palmitoyl-S-[2,3-bis(palmitoyloxy)-(2R,S)-propyl]-(R)- cysteine (Pam3Cys). The additional insertion of 6-aminohexanoic acid (Ahx) between the peptide segments and Pam3Cys further increased mitogenicity. Thus, in addition to the known mitogenic N-terminal lipopeptide of lipoprotein, additional peptide segments of the molecule were shown to exhibit a biological activity. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Circular Dichroism; Escherichia coli/metabolism; Lipoproteins/chemistry; Lipoproteins/pharmacology; Lymphocyte Activation/drug effects; Mice; Mice, Inbred BALB C; Mitogens/pharmacology; Molecular Conformation; Molecular Sequence Data; Peptides/isolation & purification; Peptides/pharmacology; Spleen/cytology; Thymidine/metabolism |
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