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  • Title: [Cloning and prokaryotic expression of recombinant Jo-1 antigen and identification of its antigen specificity].
    Author: Zhao XY, Bi ZL, Wu YH, Xin HT.
    Journal: Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi; 2008 Dec; 24(12):1170-3. PubMed ID: 19068203.
    Abstract:
    AIM: To obtain highly purified Jo-1 autoantigens. METHODS: The full length of DNA sequence coding for Jo-1 (histidyl-tRNA synthetase) was obtained from human placenta by RT-PCR and then it was inserted into pTYB11 or pMAL-c to construct the expression vectors pTYB11-Jo-1 and pMAL-c-Jo-1. The recombinant plasmids were transformed into ER2566 and BL21 of E.coli, respectively. RESULTS: The fusion Jo-1 antigens were expressed, Western blot analysis demonstrated they responded specifically to anti-Jo-1 antibody from the patients with autoimmune disease polymyositis and dermatomyositis, but did not respond to normal sera and 188 sera containing anti-RNP, Sm, Ro/La or RNP/Ro antibodies from rheumatosis patients. CONCLUSION: The expressed protein of pMAL-c-Jo-1 is soluble, which accounts for more then 50% of total proteins of cells and can be purified by affinity chromatography. The purified proteins can be used as reagents for determining the anti Jo-1 antibody in the serum of patients.
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