Work

Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin.

Year: 2018

Type: article

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: 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.

Source: Europe PMC (PubMed Central)

Authors: Samaneh Gholami, Nematolah Gheibi, Reza Falak, Koorosh Goodarzvand Chegini

Institutions: Iran University of Medical Sciences, Qazvin University of Medical Sciences

Language: English

Topic: Protein purification and stability

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

OpenAlex ID: W2767449681

FWCI: 0.468

Cites: 17

Cited by: 8

Related to: 10