[HTML][HTML] Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers
A Tsuneshige, K Kanaori, U Samuni, D Danstker… - Journal of Biological …, 2004 - ASBMB
Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
[HTML][HTML] Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers
A Tsuneshige, K Kanaori, U Samuni, D Danstker… - Journal of Biological …, 2004 - Elsevier
Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
[PDF][PDF] Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers
A Tsuneshige, K Kanaori, U Samuni, D Danstker… - 2004 - academia.edu
Chem. 277, 34508–34520). To further investigate this ef-fect in more detail,-and-
semihemoglobins, namely,(heme)(apo) and(apo)(heme), respectively, were prepared and …
semihemoglobins, namely,(heme)(apo) and(apo)(heme), respectively, were prepared and …
[引用][C] Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers
A Tsuneshige, K Kanaori, U Samuni… - Journal of Biological …, 2004 - cir.nii.ac.jp
Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond
Efficiently to Allosteric Effectors without Forming Tetramers | CiNii Research CiNii 国立情報学 …
Efficiently to Allosteric Effectors without Forming Tetramers | CiNii Research CiNii 国立情報学 …
[PDF][PDF] Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers
A Tsuneshige, K Kanaori, U Samuni, D Danstker… - 2004 - researchgate.net
Chem. 277, 34508–34520). To further investigate this ef-fect in more detail,-and-
semihemoglobins, namely,(heme)(apo) and(apo)(heme), respectively, were prepared and …
semihemoglobins, namely,(heme)(apo) and(apo)(heme), respectively, were prepared and …
Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers
A Tsuneshige, K Kanaori, U Samuni… - The Journal of …, 2004 - pubmed.ncbi.nlm.nih.gov
Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers.
A Tsuneshige, K Kanaori, U Samuni… - The Journal of …, 2004 - europepmc.org
Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers
A Tsuneshige, K Kanaori, U Samuni… - Journal of …, 2004 - einstein.elsevierpure.com
Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …