[Isolation and purification of antibacterial polypeptides from human LAK cells].
OBJECTIVE
To isolate and purify new antibiotic peptides from human lymphokine activated killer (LAK) cells.


METHODS
Preparative Acid-Urea Polyacrylamide Gel Electrophoresis and Reverse Phase HPLC were performed to isolate and purify polypeptides from the acid extract of human LAK cells. The molecule weight was analyzed by Tricine-SDS-PAGE. Radial agar diffusion assay was used to analyze the antibacterial activities.


RESULTS
Several antibiotic peptides were isolated. Two peptides were purified from fractions HLP-2, HLP-3, which had molecular weight of around 7.9 x 10(3) u and 4 x 10(3) u and were named HLP-2b and HLP-3a, respectively. Four peptides with molecular weight of 7.2 x 10(3) u, 10.4 x 10(3) u, 6.2 x 10(3) u and 6.2 x 10(3) u were almost purified and were named HLP-2a, HLP-2c, HLP-3b and HLP-3c, respectively. HLP-2b, HLP-2a, HLP-2c, HLP-3b and HLP-3c all had antimicrobial activities against S. Aureus and C. Albicans, and HLP-3a against S. Aureus only.


CONCLUSIONS
Human LAK cells contained a variety of antimicrobial peptides.
Zhang
Qi
Q
Research Unit of Infection and Immunity, West China School of Preclinical and Forensic Medicine, Sichuan University, Chengdu 610041, China.
Huang
Ning
N
Wu
Qi
Q
Wang
Boyao
B
D000900:Anti-Bacterial Agents / Q000302:isolation & purification*; D023181:Antimicrobial Cationic Peptides; D015979:Killer Cells, Lymphokine-Activated / Q000737:chemistry*; D010455:Peptides; D013211:Staphylococcus aureus / Q000187:drug effects
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; C406269:HLP-2 polypeptide; D010455:Peptides