The reactions of myoglobin, normal adult hemoglobin, sickle cell hemoglobin and hemin with hydroxyurea

被引：30

作者：

Rupon, JW

Domingo, SR

Smith, SV

Gummadi, BK

Shields, H

Ballas, SK

King, SB

Kim-Shapiro, DB ^{[1
]}

机构：

[1] Wake Forest Univ, Dept Phys, Winston Salem, NC 27103 USA

[2] Wake Forest Univ, Dept Chem, Winston Salem, NC 27103 USA

[3] Thomas Jefferson Univ, Jefferson Med Coll, Cardeza Fdn Hematol Res, Dept Med, Philadelphia, PA 19107 USA

来源：

BIOPHYSICAL CHEMISTRY | 2000年 / 84卷 / 01期

基金：

美国国家卫生研究院;

关键词：

sickle cell hemoglobin; hydroxyurea; methemoglobin; hemin; nitric oxide; time resolved absorption spectroscopy;

D O I：

10.1016/S0301-4622(99)00132-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The kinetics of the reaction of hydroxyurea (HU) with myoglobin (Mb), hemin, sickle cell hemoglobin (HbS), and normal adult hemoglobin (HbA) were determined using optical absorption spectroscopy as a function of time, wavelength, and temperature. Each reaction appeared to follow pseudo-first order kinetics. Electron paramagnetic resonance spectroscopy (EPR) experiments indicated that each reaction produced an FeNO product. Reactions of hemin and the ferric forms of HbA, HbS, and myoglobin with HU also formed the NO adduct. The formation of methemoglobin and nitric oxide-hemoglobin from these reactions may provide further insight into the mechanism of how HU benefits sickle cell patients. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：1 / 11

页数：11

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