FEBS Lett, 1987, 217(2):269-274
Detailed structural analysis of exposed domains of membrane-bound Na+, K+-ATPase A model of transmembrane arrangement
Exposed regions of the α- and β-subunits of membrane-bound Na+,K+-ATPase were in turn hydrolyzed with trypsin. Resistance of the β-subunit to proteolysis was shown to be due mainly to the presence of disulfide bridge(s) in the molecule. A model for the spatial organisation of the enzyme in the membrane was proposed on the basis of detailed structural analysis of extramembrane regions of both subunits. © 1987.
Scopus: 2-s2.0-0023225609
: 3036581
IBCH: 6202
Ссылка на статью в журнале: http://doi.wiley.com/10.1016/0014-5793%2887%2980676-2
Кол-во цитирований на 01.2024: 59
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