dc.creatorOgo S.H.
dc.creatorMatsuura M.S.A.
dc.creatorFocesi Jr. A.
dc.date1984
dc.date2015-06-30T13:43:10Z
dc.date2015-11-26T14:38:25Z
dc.date2015-06-30T13:43:10Z
dc.date2015-11-26T14:38:25Z
dc.date.accessioned2018-03-28T21:43:27Z
dc.date.available2018-03-28T21:43:27Z
dc.identifier
dc.identifierComparative Biochemistry And Physiology -- Part A: Physiology. , v. 78, n. 3, p. 587 - 589, 1984.
dc.identifier3009629
dc.identifier10.1016/0300-9629(84)90601-7
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0012278832&partnerID=40&md5=18c2d0bad791c319f57e116672135620
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/98614
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/98614
dc.identifier2-s2.0-0012278832
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1249568
dc.description1. 1. The ion-exchange Chromatographie analysis of the red cell nucleotides of two water-snakes with different degrees of adaptation to water showed a ratio ATP/GTP of about 2.3 in the more aquatic species Helicops modestus and of about 0.7 in Liophis miliaris. 2. 2. The haemoglobin oxygen affinity assayed in the presence of ATP, GTP, DPG and IHP in haemolysate from both snakes were determined as a function of pH. The Bohr effect values were always found to be increased in comparison with the stripped haemolysate, becoming about 1.5 times higher in L. miliaris compared with H. modestus by the nucleotide treatment. 3. 3. The Hill coefficient calculated from the slope of the haemoglobin binding curves was consistent with an increase in the protein cooperativity in the presence of the nucleotides assayed. The very low nH values of about 1.2 in absence of the effectors became close to 2.0 in their presence. 4. 4. The data of nucleotide Chromatographie analysis were compared to those found in fishes with bimodal respiration. © 1984.
dc.description78
dc.description3
dc.description587
dc.description589
dc.descriptionAntonini, Brunori, (1971) Haemoglobin and Myoglobin in their Reaction with Ligands, , North Holland, Amsterdam, Chap. 10
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dc.descriptionGeoghegan, Poluhowich, The major erythrocyte organic phosphate of the American eel Angilla rostrata (1974) Comp. Biochem. Physiol., 49 B, pp. 281-290
dc.descriptionKoloustian, Poluhowich, The role of organic phosphate in modulating the oxygénation behavior of eel hemoglobin (1976) Comparative Biochemistry and Physiology Part A: Physiology, 53 A, pp. 245-248
dc.descriptionMatsuura, Ogo, Focesi, Multiplicity and immunological characterization of the haemoglobin components from Liophys miliaris and Helicops modestus (1984) Comp. Biochem. Physiol., 76 B, pp. 915-919
dc.descriptionMonod, Wyman, Changeaux, On the nature of allosteric transitions: a plausible model (1965) J. molec. Biol., 12, pp. 88-118
dc.descriptionOgo, Abe, Focesi, Jr., Oxygen dissociation constant in hemoglobin of Helicops modestus and Liophys miliaris, two water snakes with different morphological adaptations to their aquatic environment (1979) Comp. Biochem. Physiol., 63 A, pp. 285-289
dc.descriptionRapoport, Guest, Distribution of acid-soluble phosphorus in the blood cells of various vertebrates (1941) J. biol. Chem., 138, pp. 269-282
dc.descriptionTrader, Frieden, Dimerization and other chemical changes in amphibian hemoglobin during meth-amorphosis (1966) J. biol. Chem., 241, pp. 357-366
dc.descriptionWeber, Lykkeboe, Johansen, Biochemical aspects of the adaptation of hemoglobin-oxygen affinity of eels to hypoxia (1975) Life Sci., 17, pp. 1345-1350
dc.descriptionWood, Johansen, Actaptation to hypoxia by increased HbO2 affinity and decreased red cell ATP concentration (1972) Nature, New Biol., 237, pp. 278-279
dc.descriptionWood, Johansen, Organic phosphate metabolism in nucleated red cells: Influence of hypoxia on eel HbO2 affinity (1973) Neth. J. Sea Res., 7, pp. 328-338
dc.descriptionWood, Johansen, Weber, Effects of ambient PO2 on hemoglobin-oxygen affinity and red cell ATP concentrations in a benthic fish, Pleuronectes platessa (1975) Respir. Physiol., 25, pp. 259-267
dc.languageen
dc.publisher
dc.relationComparative Biochemistry and Physiology -- Part A: Physiology
dc.rightsfechado
dc.sourceScopus
dc.titleContent Of Organic Polyphosphates And Their Allosteric Effects On Haemoglobins From The Water-snakes Helicops Modestus And Liophis Miliaris
dc.typeArtículos de revistas


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