Linked Life Data

8281941

Source:http://linkedlifedata.com/resource/pubmed/id/8281941

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-2-14
pubmed:databankReference
pubmed:abstractText
The complete sequence of pig lens aldose reductase (EC 1.1.1.21), a member of the nicotinamide coenzyme-dependent aldo-keto reductase super family, was determined by the combined use of data obtained from Edman degradation, fast-atom-bombardment mass spectrometry and electrospray mass spectrometry. The N-terminal residue of human and pig aldose reductase was shown to be acetylated. The assignment of a disulfide bridge (Cys298-Cys303) was obtained by mass spectrometry. Electrospray mass spectrometry has been used for molecular mass measurement of human muscle (35758 +/- 7 Da) and pig lens (35778 +/- 3Da) aldose reductase; using mild ionization conditions, it has also been used to study the reversible interaction involved in a non-covalent complex with NADP+ (36527 +/- 4Da). An alkylating analog of NADP+ (3-chloroacetylpyridine-adenine dinucleotide phosphate) was used as an irreversible inhibitor to investigate the NADP binding site and the mass of the covalent complex was measured (36521 +/- 3 Da).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
893-903
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.
pubmed:affiliation
Laboratoire de Spectrométrie de Masse Bio-Organique, URA31 CNRS, Université Louis Pasteur, Strasbourg, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't