Kinetics of domain formation by sickle hemoglobin polymers
نویسندگان
چکیده
منابع مشابه
suppression of coke formation in thermal cracking by coke inhibitors
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15 صفحه اولKinetics of the carbamylation of the amino groups of sickle cell hemoglobin by cyanate.
The NH2-terminal valine residues of both chains of oxyhemoglobin S are carbamylated 50 to 100 times faster at pH 7.4 than the a-NH2 groups of the lysine residues of the protein up to a level of 1 carbamyl group per hemoglobin molecule. The pseudo-first order rate constants for the carbamylation of the NHz-terminal residues of carbonmonoxyhemoglobins A and S are identical for the proteins either...
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متن کامل
Kinetics and Mechanism of Complex Formation between Hemoglobin and Haptoglobin*
The interaction between human hemoglobin and haptoglobin has been followed by measuring the quenching of haptoglobin fluorescence associated with complex formation. The effects of varying the concentration of the reactants suggest that hemoglobin tetramers do not react with haptoglobin, but that hemoglobin subunits are involved. Separated a! chains of hemoglobin react with haptoglobin; although...
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The primary pathogenic event of sickle cell anemia is the polymerization of the mutant hemoglobin (Hb) S within the red blood cells, occurring when HbS is in deoxy state in the venous circulation. Polymerization is known to start with nucleation of individual polymer fibers, followed by growth and branching via secondary nucleation, yet the mechanisms of nucleation of the primary fibers have ne...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1988
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(88)83020-0