Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin.

ABSTRACT: Background:Betatrophin is a member of the angiopoietin-like (ANGPTL) family that has been implicated in both triglyceride and glucose metabolism. The physiological functions and molecular targets of this protein remain largely unknown; hence, a purified available protein would aid study of the exact role of betatrophin in lipid or glucose metabolism. Methods:In this study, we cloned the full-length cDNA of betatrophin from a human liver cDNA library. Betatrophin was expressed in the pET-21b-E. coli Bl21 (DE3) system and purified by immobilized metal-affinity chromatography and ion-exchange chromatography. Results:Circular dichroism spectroscopy revealed ?-helix as the major regular secondary structure in recombinant betatrophin. Conclusion:The production method is based on commonly available resources; therefore, it can be readily implemented.

SUBMITTER: Gholami S 

PROVIDER: S-EPMC5941129 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature