Purification and characterization of a 24 kDa protein from tartary buckwheat seeds.
A 24 kDa protein was isolated from tartary buckwheat seeds by using chromatography of Superdex 75 gel filtration and Resource Q ion-exchange column. SDS-PAGE and Sephacryl S-200 gel filtration were used to provide information about the molecular mass of the protein purified from tartary buckwheat. The protein was composed of 215 amino acid residues and showed strong IgE binding activity in an ELISA test to the sera colleted from two patients allergic to buckwheat. These results suggested that the purified 24 kDa protein from tartary buckwheat seeds was an important functional protein and was relatively specific for buckwheat-allergic patients. It should be a very useful tool in the diagnosis of buckwheat allergy in the future.
College of Life Science and Biotechnology, Shanxi University, Taiyuan 030006, China. zhwang@sxu.edu.cn
Zhuanhua
Z
Wang
Zheng
Z
Zhang
Zhuohui
Z
Zhao
Gunilla
G
Wieslander
Dan
D
Norbäck
Ivan
I
Kreft
D000485:Allergens / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004797:Enzyme-Linked Immunosorbent Assay; D019612:Fagopyrum / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D006801:Humans; D007073:Immunoglobulin E / Q000097:blood; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry / Q000276:immunology / Q000378:metabolism
D000485:Allergens; D000596:Amino Acids; D010940:Plant Proteins; D007073:Immunoglobulin E