Identification of rat and human hemoglobin acetylation sites formed as a result of interaction with acetylsalicylic acid

E. V. Shreiner, E. A. Murashko, Ya A. Dubrovskii, N. V. Krasnov, E. P. Podolskaya, V. N. Babakov

Research output

Abstract

The possibility of interaction of 0.1 mg/mL acetylsalicylic acid (ASA) with purified human and rat globin proteins for 24 h in vitro was investigated. It was shown that following the interaction with ASA rat globin is modified at Lys17, Lys57, Lys91, and Lys140 amino acid residues of the α-subunit as well as at Lys18 and Lys77 of the β-subunit, whereas human globin is acetylated at Lys17, Lys41, Lys57, and Lys91 residues of the α-subunit as well as Lys18, Lys96, and Lys133 of the β-subunit of the protein. Incubation of human whole blood with 0.1 mg/mL ASA for 3 h followed by globin isolation led to the identification of acetylated Lys17 and Lys57 lysine residues of the α-subunit of human globin.

Original languageEnglish
Pages (from-to)126-132
Number of pages7
JournalRussian Journal of Bioorganic Chemistry
Volume38
Issue number2
DOIs
Publication statusPublished - 1 Mar 2012

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Acetylation
Forensic Anthropology
Globins
Aspirin
Rats
Hemoglobins
Protein Subunits
Lysine
Blood
Amino Acids
Proteins

Scopus subject areas

  • Biochemistry
  • Organic Chemistry

Cite this

Shreiner, E. V. ; Murashko, E. A. ; Dubrovskii, Ya A. ; Krasnov, N. V. ; Podolskaya, E. P. ; Babakov, V. N. / Identification of rat and human hemoglobin acetylation sites formed as a result of interaction with acetylsalicylic acid. In: Russian Journal of Bioorganic Chemistry. 2012 ; Vol. 38, No. 2. pp. 126-132.
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Identification of rat and human hemoglobin acetylation sites formed as a result of interaction with acetylsalicylic acid. / Shreiner, E. V.; Murashko, E. A.; Dubrovskii, Ya A.; Krasnov, N. V.; Podolskaya, E. P.; Babakov, V. N.

In: Russian Journal of Bioorganic Chemistry, Vol. 38, No. 2, 01.03.2012, p. 126-132.

Research output

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