Reports of Biochemistry

Mendeley  

Zotero  

Gholami S, Gheibi N, Falak R, Goodarzvand Chegini K. Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin. rbmb.net 2018; 6 (2) :158-163
URL: http://rbmb.net/article-1-162-en.html

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. 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. Circular dichroism spectroscopy revealed α-helix as the major regular secondary structure in recombinant betatrophin. The production method is based on commonly available resources; therefore, it can be readily implemented.