Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/97805
Type: Artigo de periódico
Title: Oxygen Dissociation Constants In Haemoglobins Of Helicops Modestus And Liophis Miliaris, Two Water-snakes With Different Morphological Adaptations To Their Aquatic Environment
Author: Ogo S.H.
Abe A.S.
Focesi Jr. A.
Abstract: 1. 1.Both Helicops modestus and Liophis miliaris. Brasilian water snakes with different degrees of aquatic adaptations, present 3 haemoglobin components identified by starch-gel electrophoresis and separated by DEAE-Sephadex A-50 and CM-cellulose chromatography respectively. 2. 2.Some functional properties of their haemoglobins were determined. Both the oxygen affinity 1.0mmHg at pH 7) and the alcaline Bohr effect value (-0.07) of the stripped haemoglobins of the more aquatic species H. modestus were higher than those of L. miliaris (1.4mmHg and -0.30 respectively). 3. 3.The ATP effect on both haemoglobin-oxygen affinity and Bohr effect was more pronounced in L. miliaris haemoglobins. The values found were 17.8mmHg at pH 7 and -0.9; in H. modestus. they were 8.93 mmHg and -0.55. 4. 4.Nucleotide triphosphate concentrations were determined as 2.84 mmHg in H. modrstus and 2.65 mM in L. miliaris (whole blood); haemoglobin concentrations were 6.14mM and 4.21 mM (as haem), respectively. The physiological implications of these results are discussed. © 1979.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/0300-9629(79)90161-0
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0018406467&partnerID=40&md5=a955a5ce607e88e38e871a5d659d90dd
Date Issue: 1979
Appears in Collections:Unicamp - Artigos e Outros Documentos

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