Ontology highlight
ABSTRACT: Background
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.Methods
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.Results
Circular dichroism spectroscopy revealed α-helix as the major regular secondary structure in recombinant betatrophin.Conclusion
The production method is based on commonly available resources; therefore, it can be readily implemented.
SUBMITTER: Gholami S
PROVIDER: S-EPMC5941129 | biostudies-literature | 2018 Apr
REPOSITORIES: biostudies-literature

Reports of biochemistry & molecular biology 20180401 2
<h4>Background</h4>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.<h4>Methods</h4>In this study, we cloned the full-length cDNA of betatrophin from a human liver cDNA library. Betatrophin was expressed in t ...[more]