Polyphosphate Binding Sites In Liophis Miliaris Hemoglobin. Evidence With Reduced Nicotinamide Adenine Dinucleotide Phosphate.

dc.creatorFocesi Junior A.
dc.creatorTakagi M.
dc.creatorOgo S.H.
dc.date1990
dc.date2015-06-30T14:01:02Z
dc.date2015-11-26T14:40:32Z
dc.date2015-06-30T14:01:02Z
dc.date2015-11-26T14:40:32Z
dc.date.accessioned2018-03-28T21:46:50Z
dc.date.available2018-03-28T21:46:50Z
dc.identifier
dc.identifierAnais Da Academia Brasileira De Ciencias. , v. 62, n. 4, p. 401 - 408, 1990.
dc.identifier13765
dc.identifier
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0025525971&partnerID=40&md5=16214781c115a850be923deec9ef18c2
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/98917
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/98917
dc.identifier2-s2.0-0025525971
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1250444
dc.descriptionThe water-snake Liophis miliaris presents hemoglobin which binds organic polyphosphate through a simple single-site per tetramer (Mol. Wt. 64500) as judged by titration curves of reduced nicotinamide adenine dinucleotide phosphate either in the presence or absence of inositol hexaphosphate. The site seems to have the same structural nature of that found on other hemoglobins and is able to strongly bind most of the known protein effectors such as inositol hexaphosphate, adenosine triphosphate or 2,3-diphosphoglicerate. The high association constant at pH 7 of reduced nicotinamide for the deoxy hemoglobin of about K(D) = 7 x 10(6) M-1 compared to human hemoglobin (K(D) = 7 x 10(5) M-1), and to that of adenosine triphosphate (its natural erythrocytic polyphosphate) still higher of about K(D) = 10(11) M-1, shows clearly the very high affinity of this snake hemoglobin for such allosteric effector. The results besides corroborating the dimer-tetramer transition mechanism proposed to describe the oxygen transport by the hemoglobin of Liophis miliaris--may explain the difficulties to obtain the oxy dimeric conformation of the protein by usual hemolysis and stripped off procedures.
dc.description62
dc.description4
dc.description401
dc.description408
dc.languageen
dc.publisher
dc.relationAnais da Academia Brasileira de Ciencias
dc.rightsaberto
dc.sourceScopus
dc.titlePolyphosphate Binding Sites In Liophis Miliaris Hemoglobin. Evidence With Reduced Nicotinamide Adenine Dinucleotide Phosphate.
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución