A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2

A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2

Proteases catalyse irreversible posttranslational modifications that often alter a biological function of the substrate. The protease dipeptidyl peptidase 4 (DPP4) is a pharmacological target in type 2 diabetes therapy primarily because it inactivates glucagon-like protein-1. DPP4 also has roles in...

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Bibliographic Details
Main Authors: Cecy R Xi, Arianna Di Fazio, Naveed Ahmed Nadvi, Karishma Patel, Michelle Sui Wen Xiang, Hui Emma Zhang, Chandrika Deshpande, Jason K K Low, Xiaonan Trixie Wang, Yiqian Chen, Christopher L D McMillan, Ariel Isaacs, Brenna Osborne, Ana Júlia Vieira de Ribeiro, Geoffrey W McCaughan, Joel P Mackay, W Bret Church, Mark D Gorrell
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:Molecules
Subjects:
recombinant protein
protease
DPP4
Covid-19
Online Access:https://www.mdpi.com/1420-3049/25/22/5392

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https://www.mdpi.com/1420-3049/25/22/5392

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