Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Cristina L. Nagatomo"'
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 109:701-707
The hemoglobins of three snake species: Liophis miliaris, Bothrops alternatus and Boa constrictor present a single ATP binding site per tetramer. The ATP association constant values for the deoxyhemoglobins at pH 7.5 were about KD ≅ 106 M−1 (107
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59fc9fe503a480b250cc4b9419629d3f
https://doi.org/10.1016/0305-0491(94)90133-3
https://doi.org/10.1016/0305-0491(94)90133-3
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 105:271-275
Bothrops alternatus oxyhemolysate showed two components by DE-52 cellulose ion- exchange chromatography and polyacrylamide gel electrophoresis: Hb I representing 70% of the bemolysate and Hb II (30%); both are dimeric in the stripped form (mol.wt 32,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0e88fcdde680969df15eb79cc868b2b
https://doi.org/10.1016/0305-0491(93)90228-w
https://doi.org/10.1016/0305-0491(93)90228-w
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 103:985-989
1. 1. The primitive snake Boa constrictor presents in the stripped hemolysate one component which from O2, equilibrium curves produced the following values: log P50 ± −0.1 and Hill coefficient nH = 1.1, independent of pH. 2. 2. Bothrops alternatus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c12ccb2244d4cef14d0ed3683eca044f
https://doi.org/10.1016/0305-0491(92)90227-i
https://doi.org/10.1016/0305-0491(92)90227-i