کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5131721 | 1491328 | 2017 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
This report establishes a correlation between two known properties of the human embryonic hemoglobins-- their weak subunit assemblies as demonstrated here by gel filtration at very dilute protein concentrations and their high oxygen affinities and reduced cooperativities reported previously by others but without a mechanistic basis. We demonstrate here that their high oxygen affinities are a consequence of their weak assemblies. Weak vs strong hemoglobin tetramers represent a regulatory mechanism to modulate oxygen binding capacity by altering the equilibrium between the various steps in the assembly process that can be described as an inverse allosteric effect.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 519, 15 February 2017, Pages 38-41
Journal: Analytical Biochemistry - Volume 519, 15 February 2017, Pages 38-41
نویسندگان
Lois R. Manning, Anthony M. Popowicz, Julio C. Padovan, Brian T. Chait, James M. Manning,