AU - Gholami, Samaneh AU - Gheibi, Nematolah AU - Falak, Reza AU - Goodarzvand Chegini, Koorosh TI - Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin PT - JOURNAL ARTICLE TA - rbmb JN - rbmb VO - 6 VI - 2 IP - 2 4099 - http://rbmb.net/article-1-162-en.html 4100 - http://rbmb.net/article-1-162-en.pdf SO - rbmb 2 ABĀ  - 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. CP - IRAN IN - Tel: +98 9113372505; Fax: +98 281 3324970 LG - eng PB - rbmb PG - 158 PT - Original Article YR - 2018