@ARTICLE{Goodarzvand Chegini, author = {Gholami, Samaneh and Gheibi, Nematolah and Falak, Reza and Goodarzvand Chegini, Koorosh and }, title = {Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin}, volume = {6}, number = {2}, abstract ={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. }, URL = {http://rbmb.net/article-1-162-en.html}, eprint = {http://rbmb.net/article-1-162-en.pdf}, journal = {Reports of Biochemistry and Molecular Biology}, doi = {}, year = {2018} }