Membrane and Secretory Protein Extraction of Mycobacterium Tuberculosis and Mycobacterium Bovis Using One Dimensional Electrophoresis (SDS-PAGE)

<p>Background & Aim: Despite the drug resistance M.bovis and Mycobacterium tuberculosis (MTB) are still regarded as two of the global health problems in the world. In the present study, a comparison was made between protein profiles of M.bovis and MTB in order to achieve effective biomarke...

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Main Authors: M K Sharifi Yazdi (Author), Mohammad Khalifeh-Gholi (Author), H Choobineh (Author), A Hadizadeh Tasbiti (Author), S Sharifi Yazdi (Author), Sh Yari (Author)
Format: Book
Published: Journal of Clinical Microbiology and Biochemical Technology - Peertechz Publications, 2017-06-30.
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Summary:<p>Background & Aim: Despite the drug resistance M.bovis and Mycobacterium tuberculosis (MTB) are still regarded as two of the global health problems in the world. In the present study, a comparison was made between protein profiles of M.bovis and MTB in order to achieve effective biomarkers for diagnosis of TB. The clinical samples, sputum and gastric lavage (and the other samples) were processed by N-acetyl-Lcysteine-sodium hydroxide methods and consequently were cultured on Lowenstein-Jensen medium. Mycobacterium tuberculosis and bovis strains were distinguished according to the biochemical tests and susceptibility testing system. Colonies were grown in 7H9 medium and membrane and secretory proteins were extracted, purifi ed by ammonium sulfate and refrigerated alcohol methods. The protein contents were measured by Bradford method. Comparison of protein bands in each strain were performed by one dimensional electrophoresis. The major discrepancy between the two strains in the banding separation membrane proteins could be observed in 45 and 60 KDa and also less than 45 and 14 KDa. The results showed that discrepancy in the proteins bands could be used as protein effective biomarker for TB diagnosis. We should use antibody against TB for further investigation for rapid TB diagnosis</p>
DOI:10.17352/jcmbt.000025