These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Study on the effect of aluminum (III) on NADH in the presence of NH4Ac in aqueous solution].
    Author: Yang XD, Miao Q, Qian SL, Bi SP.
    Journal: Guang Pu Xue Yu Guang Pu Fen Xi; 2005 Jan; 25(1):79-82. PubMed ID: 15852825.
    Abstract:
    This paper studied the interactions of Al (III ) and dihydronicotinamide adenine dinucleotide (NADH) in nearly neutral aqueous solutions (pH 6.5) by means of UV-Vis and 1H, 13C-NMR techniques. The results suggested that Al (III) interacts with NADH to form Al-NADH complexes by occupying the binding sites of phosphate oxygen atoms O(N)1 and O(A)1 and ribose ring hydroxyl groups, which are the potential recognition sites for substrates, coenzyme and enzyme. In the presence of NH4Ac salt buffer and with Al (III) salt solution, NADH will be marked with structural changes at the nicotinamide moiety in contrast with almost no structural changes in Tris-HCl buffer solution with Al (III) salt.
    [Abstract] [Full Text] [Related] [New Search]