Linked Life Data

8281941

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

Statements in which the resource exists.
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pubmed-article:8281941pubmed:abstractTextThe 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).lld:pubmed
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pubmed-article:8281941pubmed:year1993lld:pubmed
pubmed-article:8281941pubmed:articleTitleSequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.lld:pubmed
pubmed-article:8281941pubmed:affiliationLaboratoire de Spectrométrie de Masse Bio-Organique, URA31 CNRS, Université Louis Pasteur, Strasbourg, France.lld:pubmed
pubmed-article:8281941pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8281941pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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