Please use this identifier to cite or link to this item:
|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|
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.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.