en بیوشیمی Biochemistry مقالات اصلی Original Article <div style="text-align: justify;">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 &alpha;-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.</div> CD spectroscopy, Human betatrophin, Recombinant protein 158 163 http://rbmb.net/browse.php?a_code=A-10-85-1&slc_lang=en&sid=1 Samaneh Gholami Sama.gholami63@gmail.com 10031947532846006286 10031947532846006286 No Department of Biotechnology, Qazvin University of Medical Sciences, Qazvin, Iran-Immunology Research Center, Iran University of Medical Sciences, Tehran, Iran Nematolah Gheibi kgchegini@qums.ac.ir 10031947532846006287 10031947532846006287 No Department of Biotechnology, Qazvin University of Medical Sciences, Qazvin, Iran. Reza Falak Falak.r@iums.ac.ir 10031947532846006288 10031947532846006288 No Immunology Research Center, Iran University of Medical Sciences, Tehran, Iran. Koorosh Goodarzvand Chegini kgchegini@qums.ac.ir 10031947532846006289 10031947532846006289 Yes Department of Clinical Biochemistry and Genetics, Qazvin University of Medical Sciences, Qazvin, Iran.