Linked Life Data

6861757

Source:http://linkedlifedata.com/resource/pubmed/id/6861757

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-8-26
pubmed:abstractText
Subunit II (with a molecular mass of about 24000 dalton, approximately 24 kDA) of NADH dehydrogenase from beef heart mitochondria was [ 14C ]carboxymethylated and cleaved with CNBr and proteolytic enzymes. Sequence analyses of purified fragments suggest that the subunit is composed of a homogeneous polypeptide chain, containing just over 230 residues. The primary structure of this chain was established except for a 14-residue internal part which was only determined by composition. The amino acid sequence suggests that four cysteine residues are involved in the binding of an iron-sulfur cluster. The subunit contains no long hydrophobic segment, in contrast to structures often found in membrane proteins, but in agreement with a model where the functional unit of NADH dehydrogenase in the membrane is shielded by other intra-membrane proteins. The polypeptide has a weak similarity to the iron-sulfur binding region of ferredoxin and has interesting but possibly insignificant similarities to parts of previously compared flavin-linked enzymes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-50
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
The primary structure of subunit II of NADH dehydrogenase from bovine-heart mitochondria.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't