A New Functional Model for Prediction of Chaperone Activity of the Recombinant M. tb Acr (α-Crystallin) Using Insulin as Substrate.

ABSTRACT: Mycobacterium tuberculosis Acr is an important protein expressed in latent tuberculosis which is active as an oligomer in preventing misfolding of cellular proteins. In this study, Mycobacterium alpha crystallin (acr) gene was cloned and expressed in Escherichia coli (E. coli). The recombinant Acr protein was purified by Nickel-NTA resin. The oligomeric state of Acr was confirmed by gel filtration chromatography using Sephacryl S-200 and Native-PAGE. Studies of chaperone activity were performed with insulin as a substrate at different mole ratios of Acr with 2 types of samples, His tag elutes (H) and His tag elutes with gel filtration (G). It was observed that the ratio of different sizes of oligomers (9 to 24 mers) had a significant effect on chaperone activity. Using

SUBMITTER: Krishnan G 

PROVIDER: S-EPMC6387734 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature