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Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.

Eur. J. Biochem.1993 Dec 15;218(3):893-903. doi:10.1111/j.1432-1033.1993.tb18445.x
M Jaquinod 1 , N Potier , K Klarskov , J M Reymann , O Sorokine , S Kieffer , P Barth , V Andriantomanga , J F Biellmann , A Van Dorsselaer
M Jaquinod 1 , N Potier , K Klarskov , J M Reymann , O Sorokine , S Kieffer , P Barth , V Andriantomanga , J F Biellmann , A Van Dorsselaer
+ et al

[No authors listed]

Author information
  • 1 Laboratoire de Spectrométrie de Masse Bio-Organique, URA31 CNRS, Université Louis Pasteur, Strasbourg, France.

摘要


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).