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Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers.
Tsuneshige A, Kanaori K, Samuni U, Danstker D, Friedman JM, Neya S, Giangiacomo L, Yonetani T. Tsuneshige A, et al. Among authors: yonetani t. J Biol Chem. 2004 Nov 19;279(47):48959-67. doi: 10.1074/jbc.M405909200. Epub 2004 Sep 10. J Biol Chem. 2004. PMID: 15361521 Free article.
Significant reduction in oxygen affinity resulting from interactions between heterotropic allosteric effectors and hemoglobin in not only the unligated derivative but also the fully ligated form has been reported (Tsuneshige, A., Park, S. I., and Yonetani, T. (2002) …
Significant reduction in oxygen affinity resulting from interactions between heterotropic allosteric effectors and hemoglobin in not only th …
224 results