Volume 6, Issue 2 (Vol.6 No.2 Apr 2018)                   rbmb.net 2018, 6(2): 158-163 | Back to browse issues page

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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
Department of Clinical Biochemistry and Genetics, Qazvin University of Medical Sciences, Qazvin, Iran.
Abstract:   (4300 Views)
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.
Full-Text [PDF 437 kb]   (1521 Downloads)    
Type of Article: Original Article | Subject: Biochemistry
Received: 2017/04/27 | Accepted: 2017/06/16 | Published: 2017/10/1

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