Reductive nitrosylation of ferric human serum heme-albumin
نویسندگان
چکیده
منابع مشابه
Human serum albumin modifications associated with reductive radical stress.
Radiation-induced modifications of human serum albumin mainly occurring at S-containing residues were investigated by Raman spectroscopy and mass spectrometry techniques. When HO˙ radicals were scavenged by t-BuOH, the H˙ atom and hydrated electron (e(aq)(-)) attack led to the chemical transformation of Cys into Ala residues and the conversion of Met residues into α-aminobutyric acid residues. ...
متن کاملReductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation.
Cyanide binds to ferric heme-proteins with a very high affinity, reflecting the very low dissociation rate constant (k(off)). Since no techniques are available to estimate k(off), we report herewith a method to determine k(off) based on the irreversible reductive nitrosylation reaction to trap ferric myoglobin (Mb(III)). The k(off) value for cyanide dissociation from ferric cyanide horse heart ...
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متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2010
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2010.07662.x