Isolation and purification of antimicrobial polypeptide HMGN2 from human lymph node and analysis of its distribution.
- Author:
Wei LI
1
;
Ping ZHANG
;
Xiangli KONG
;
Yan LI
;
Sixu CHEN
;
Yun FENG
;
Qi WU
;
Boyao WANG
Author Information
1. Department of Dermatovenereology, West China Hospital, Sichuan University, Chengdu 610041, China.
- Publication Type:Journal Article
- MeSH:
Antimicrobial Cationic Peptides;
isolation & purification;
metabolism;
Escherichia coli;
drug effects;
HMGN2 Protein;
isolation & purification;
metabolism;
Humans;
Lymph Nodes;
chemistry;
metabolism;
Tissue Distribution
- From:
Journal of Biomedical Engineering
2010;27(4):842-846
- CountryChina
- Language:Chinese
-
Abstract:
This study was conducted to isolate and purify antimicrobial polypeptides HMGN2 (high mobility group nucleosomal-binding domain2) from human lymph node, to detect the antimicrobial activity of HMGN2, and to determine the subcellular location of HMGN2 in human lymph node. The antimicrobial polypeptides were purified by the Reverse Phase HPLC and identified by Tricine-SDS-PAGE. The antimicrobial activity was detected by agar diffusion test. Mass spectrum and Western-blot analysis indicated the individual character of protein. HMGN2 was isolated and purified from human lymph node, and it showed antimicrobial potency against the pathogenic strain E. coli 54,080. The immunocytochemistry staining indicated that HMGN2 was present both in human lymph node cells' nucleus and cytoplasm. In conclusion, HMGN2 protein is of antimicrobial activity and it is probably involved in the defence of innate immunity in vivo.
