Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/98282
Type: Artigo de periódico
Title: Fluorescence Studies On The Binding Of Reduced Nicotinamide Adenine Dinucleotide Phosphate To Human Hemoglobin A And Its Variant Hemoglobin Providence.
Author: Ogo S.H.
Focesi Junior A.
Cashon R.
Bonaventura C.
Bonaventura J.
Abstract: The affinity constants for the binding of NADPH to human hemoglobin A were directly determined by fluorescence analysis since nucleotide fluorescence is quenched on binding to the protein. The binding constants 6.1 x 10(5), 5.02 x 10(5) and 1.2 x 10(5) were found for deoxyhemoglobin at pH 6.5, 7.0 and 7.5, respectively. Oxyhemoglobin does not bind NADPH significantly. These results are consistent with those found in oxygen-hemoglobin equilibrium experiments. The human hemoglobin variant, Providence-Asp, which has a marked decrease in 2,3 DPG affinity was also investigated. NADPH does not bind to the variant suggesting that the Lys B 82 residue is of fundamental importance to nucleotide binding and showing that the binding site is the same as that of 2,3 DPG or other organic polyphosphate, allosteric modulators of hemoglobins. Experiments of inositol hexaphosphate (IHP)-NADPH site competition corroborate these results.
Editor: 
Rights: aberto
Identifier DOI: 
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0023514558&partnerID=40&md5=6e852c68c6b6a5098b42ca32c330fe52
Date Issue: 1987
Appears in Collections:Unicamp - Artigos e Outros Documentos

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