ZG16p, an Animal Homologue of Plant β-Prism Fold Lectins: Purification Methods of Natural and Recombinant ZG16p and Inhibition Assay of Cancer Cell Growth Using ZG16p

Autor:	Akiko, Mito, Kaori, Kumazawa-Inoue, Kyoko, Kojima-Aikawa
Rok vydání:	2020
Předmět:	Models Molecular Protein Conformation Lectins Escherichia coli Animals Humans Drug Screening Assays Antitumor HCT116 Cells Protein Engineering Pancreas Recombinant Proteins Cell Proliferation Rats
Zdroj:	Methods in molecular biology (Clifton, N.J.). 2132
ISSN:	1940-6029
Popis:	ZG16p is a soluble 16-kDa protein abundantly expressed in the pancreas and gut, and has a β-prism fold structure similar to that of mannose-binding Jacalin-related lectins (mJRLs) such as BanLec, Heltuba, and Artocarpin. ZG16p binds to mannose via the well-conserved GXXXD loop among mJRLs and sulfated glycosaminoglycans (e.g., heparin and heparan sulfate) via the basic patch of molecular surface. In addition to the above binding activities, ZG16p has inhibitory activity against proliferation of colon cancer cells. This manuscript describes purification of rat pancreatic ZG16p and recombinant ZG16p expressed in Escherichia coli expression system, and cell growth inhibition assay using ZG16p as an inhibitor.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::12c760bae430cdfe3b2e3d03a0020bb0 https://pubmed.ncbi.nlm.nih.gov/32306341 Zobrazit plný text záznamu