| Literature DB >> 3036581 |
N M Arzamazova, E A Arystarkhova, N M Gevondyan, N A Aldanova, N N Modyanov.
Abstract
Exposed regions of the alpha- and beta-subunits of membrane-bound Na+,K+-ATPase were in turn hydrolyzed with trypsin. Resistance of the beta-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.Entities:
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Year: 1987 PMID: 3036581 DOI: 10.1016/0014-5793(87)80676-2
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124