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- W2360757965 abstract "Objective To purify native and recombinant heparin-binding haemagglutinin(HBHA) proteins,and investigate the application value in clinical diagnosis of tuberculosis.Methods The HBHA gene was amplified by polymerase chain reaction with specific primers from genomic DNA of Mycobacterium tuberculosis H37Rv strain,and was inserted into the cloning and expression vector PQE80L.After sequencing,it was transferred into the host strain Escherichia coli BL-21,and then induced by isopropyl-β-D-1-thogal actopyranoside(IPTG) to express HBHA protein.After the expressed protein was analyzed by SDS-PAGE and Western blot,it was purified by affinity chromatography.The polyclonal antibody was prepared by immunizing New-Zealand rabbit.After growing bacille calmette-guerin(BCG) to the stationary status in the 7H9 liquid medium,the native HBHA protein was obtained by CL-6B column chromatography.The antibody′s activity was determined in inhibiting BCG aggregation induced by native HBHA and recombinant HBHA.Results The native and recombinant HBHA proteins could induce the BCG aggregation,which could be inhibited by both polyclonal antibodies.Conclusions The native and recombinant HBHA proteins are successfully obtained.It is proved that the recombinant HBHA protein could induce the aggregation of BCG as similar as native HBHA protein,and polyclonal antibody against recombinant HBHA protein could be also inhibit the activity of native HBHA protein.It suggests that HBHA could be further used in clinical diagnosis and research of HBHA." @default.
- W2360757965 created "2016-06-24" @default.
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- W2360757965 date "2011-01-01" @default.
- W2360757965 modified "2023-09-26" @default.
- W2360757965 title "Research on the application of HBHA protein in the diagnosis of tuberculosis" @default.
- W2360757965 hasPublicationYear "2011" @default.
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