scholarly journals Neurochemical Characterization of Zinc Transporter 3-Like Immunoreactive (ZnT3+) Neurons in the Intramural Ganglia of the Porcine Duodenum

2012 ◽  
Vol 48 (3) ◽  
pp. 766-776 ◽  
Author(s):  
Joanna Wojtkiewicz ◽  
Sławomir Gonkowski ◽  
Maciej Równiak ◽  
Robert Crayton ◽  
Mariusz Majewski ◽  
...  
Keyword(s):  
Zinc Transporter ◽  
Intramural Ganglia

scholarly journals Functional Characterization of a Novel Mammalian Zinc Transporter, ZnT6

2002 ◽  
Vol 277 (29) ◽  
pp. 26389-26395 ◽  
Author(s):  
Liping Huang ◽  
Catherine P. Kirschke ◽  
Jane Gitschier
Keyword(s):  
Functional Characterization ◽  
Zinc Transporter

Characterization of the GufA subfamily member SLC39A11/Zip11 as a zinc transporter

2013 ◽  
Vol 24 (10) ◽  
pp. 1697-1708 ◽  
Author(s):  
Yu Yu ◽  
Aimin Wu ◽  
Zhuzhen Zhang ◽  
Guang Yan ◽  
Fan Zhang ◽  
...  
Keyword(s):  
Zinc Transporter ◽  
Subfamily Member

Characterization of a vacuolar zinc transporter OZT1 in rice (Oryza sativa L.)

2012 ◽  
Vol 40 (2) ◽  
pp. 1201-1210 ◽  
Author(s):  
Hong-Xia Lan ◽  
Zhou-Fei Wang ◽  
Qi-Hong Wang ◽  
Mei-Mei Wang ◽  
Yong-Mei Bao ◽  
...  
Keyword(s):  
Oryza Sativa ◽  
Oryza Sativa L ◽  
Zinc Transporter

scholarly journals Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain

2021 ◽  
Vol 9 ◽  
Author(s):  
Camila A. Cotrim ◽  
Russell J. Jarrott ◽  
Andrew E. Whitten ◽  
Hassanul G. Choudhury ◽  
David Drew ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Biochemical Characterization ◽  
Expression System ◽  
Zinc Transporter ◽  
X Ray ◽  
Terminal Domain ◽  
X Ray Scattering ◽  
Cholesteryl Hemisuccinate ◽  
Soluble C

Human zinc transporter 1 (hZnT1) belongs to the cation diffusion facilitator (CDF) family. It plays a major role in transporting zinc (Zn2+) from the cytoplasm across the plasma membrane and into the extracellular space thereby protecting cells from Zn2+ toxicity. Through homology with other CDF family members, ZnT1 is predicted to contain a transmembrane region and a soluble C-terminal domain though little is known about its biochemistry. Here, we demonstrate that human ZnT1 and a variant can be produced by heterologous expression in Saccharomyces cerevisiae cells and purified in the presence of detergent and cholesteryl hemisuccinate. We show that the purified hZnT1 variant has Zn2+/H+ antiporter activity. Furthermore, we expressed, purified and characterized the soluble C-terminal domain of hZnT1 (hZnT1-CTD) in a bacterial expression system. We found that the hZnT1-CTD melting temperature increases at acidic pH, thus, we used an acetate buffer at pH 4.5 for purifications and concentration of the protein up to 12 mg/mL. Small-angle X-ray scattering analysis of hZnT1-CTD is consistent with the formation of a dimer in solution with a V-shaped core.

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