Antibody preparation and enzyme linked immunosorbent assay of Lonicera japonica phenylalnine ammonia lyase.
- Author:
Zhou-yong WANG
1
;
Lu-qi HUANG
1
;
Yuan YUAN
1
;
Bao-min WANG
2
Author Information
1. National Resource Center for Chinese Materia Medica, Chinese Academy of Chinese Medical Sciences, Beijing 100700, China.
2. China Agriculture University, Beijing 100094, China.
- Publication Type:Journal Article
- MeSH:
Antibodies;
immunology;
metabolism;
Antibody Specificity;
Blotting, Western;
Enzyme-Linked Immunosorbent Assay;
Escherichia coli;
genetics;
metabolism;
Flowers;
chemistry;
Gene Expression Regulation, Plant;
Genetic Vectors;
Lonicera;
chemistry;
Phenylalanine Ammonia-Lyase;
chemistry;
immunology;
isolation & purification;
Plants, Medicinal;
chemistry;
Plasmids;
Protein Structure, Secondary;
Protein Structure, Tertiary
- From:
Acta Pharmaceutica Sinica
2013;48(9):1498-1502
- CountryChina
- Language:Chinese
-
Abstract:
The expression of phenylalnine ammonia lyase (LJPAL1) is closely related to the content of active compounds in Lonicera japonica. In this paper, a prokaryotic expression vector is constructed and LJPAL1 protein is expressed in E. coli. Three antigen sites were synthesized to peptide antigen and prepared polyclonal antibody of Anti-LJT-1, Anti-LJT-2 and Anti-LJT-3, separately. Antibody Anti-LJT-2 was screened using Western blotting. And indirect ELISA was built using Anti-LJT-2. The results of this study will be a base for honeysuckle chemical quality and evaluation kits.
