Localization of Na+-K+ ATPases in Quasi-Native Cell Membranes


Autoria(s): Jiang JG; Hao X; Cai MJ; Shan YP; Shang X; Tang ZY; Wang HD
Data(s)

2009

Resumo

Na+-K+ ATPases have been observed and located by in situ AFM and single molecule recognition technique, topography and recognition imaging (TREC) that is a unique technique to specifically identify single protein in complex during AFM imaging. Na+-K+ ATPases were well distributed in the inner leaflet of cell membranes with about 10% aggregations in total recognized proteins. The height of Na+-K+ ATPases measured by AFM is in the range of 12-14 nm, which is very consistent with the cryoelectron microscopy result. The unbinding force between Na+-K+ ATPases in the membrane and anti-ATPases on the AFM tip is about 80 pN with the apparent loading rate at 40 nN/s.

Identificador

http://202.98.16.49/handle/322003/11417

http://www.irgrid.ac.cn/handle/1471x/147947

Idioma(s)

英语

Fonte

Jiang JG;Hao X;Cai MJ;Shan YP;Shang X;Tang ZY;Wang HD.Localization of Na+-K+ ATPases in Quasi-Native Cell Membranes,NANO LETTERS,2009,9(12):4489-4493

Palavras-Chave #ATOMIC-FORCE MICROSCOPY #DNA #COMPLEX #CFTR
Tipo

期刊论文