Gel Protein Extraction's Impact on Conformational Epitopes of Linear Non-Tagged MPT64 Protein.

ABSTRACT: The production and purification of recombinant proteins are crucial to acquiring pure MPT64 protein. Due to the fact that protein epitopes may undergo conformational changes during purification, this study, therefore, investigated an effective rapid purification method to produce highly intracellular pure MPT64 protein without causing conformational changes in the epitope under denaturing conditions. MPT64 was isolated from E. coli and electrophoresed using gel SDS-PAGE. Then, the desired protein bands were excised and purified with two methods: electroelution and passive elution. The isolated protein was identified via peptide mass fingerprinting using MALDI-TOF MS and reacted with IgG anti-MPT64, and the cross-reactivity of the isolated protein with IgY anti-MPT64 was confirmed us

SUBMITTER: Kusuma SAF 

PROVIDER: S-EPMC10378983 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature