Linked Life Data

1333160

Source:http://linkedlifedata.com/resource/pubmed/id/1333160

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1992-12-30
pubmed:abstractText
The organization of the hydrophobic domain of the Na,K-ATPase in the E1 and E2 form of the enzyme has been studied by labelling with two hydrophobic photoactivable reagents 3-(trifluoromethyl)-3-(m-[125I]iodophenyl) diazirine ([125I]TID) and 1-palmitoyl-2-[11-[4-[3-(trifluoromethyl) diazirinyl] phenyl] [2-3H]undecanoyl]-sn-glycero-3-phosphorylcholine ([3H]PTPC/11). The incorporation of the reagents into the alpha-subunit but not into the beta-subunit in the E1-conformation was shown to be lower than that in the E2 form. This indicated the structural rearrangement of the alpha-subunit, which resulted in a change in the accessibility of the membrane-bound fragments for the hydrophobic labels. The set of the [125I]TID-labelled peptides of the alpha-subunit was shown to be the same for the E1 and E2 form of the enzyme: Asp68-Lys142, Ile265-Lys341, Val545-Lys589, Ser770-Lys826, Leu842-Arg880, Asn936-Arg972 and Met973-Arg999, which points to the different level of modification of the same fragments. The first results of molecular modelling of the spatial organization of the intramembrane part of Na+,K(+)-ATPase are also presented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0302-2994
pubmed:author
pubmed:issnType
Print
pubmed:volume
607
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-58
pubmed:dateRevised
2008-2-20
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Transmembrane organization of the Na+,K(+)-ATPase molecule.
pubmed:affiliation
Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
pubmed:publicationType
Journal Article