Title of article
Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin
Author/Authors
Goodarzvand Chegini , Koorosh Department of Clinical Biochemistry and Genetics - Qazvin University of Medical Sciences - Qazvin, Iran , Gholami , Samaneh Department of Biotechnology - Qazvin University of Medical Sciences - Qazvin, Iran , Gheibi , Nematolah Department of Biotechnology - Qazvin University of Medical Sciences - Qazvin, Iran , Falak , Reza Immunology Research Center - Iran University of Medical Sciences - Tehran, Iran
Pages
6
From page
158
To page
163
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.
Keywords
Recombinant protein , Human betatrophin , CD spectroscopy
Journal title
Reports of Biochemistry and Molecular Biology (RBMB)
Serial Year
2018
Record number
2525218
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