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

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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.

в: Russian Journal of Bioorganic Chemistry, Том 38, № 2, 01.03.2012, стр. 126-132.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Author

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. в: Russian Journal of Bioorganic Chemistry. 2012 ; Том 38, № 2. стр. 126-132.

BibTeX

@article{f9af841355054a55ae86450967c1c8eb,

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

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.",

keywords = "Acetylation, Acetylsalicylic acid, Aspirin, Hemoglobin, MALDI-TOF",

author = "Shreiner, {E. V.} and Murashko, {E. A.} and Dubrovskii, {Ya A.} and Krasnov, {N. V.} and Podolskaya, {E. P.} and Babakov, {V. N.}",

year = "2012",

month = mar,

day = "1",

doi = "10.1134/S1068162012020094",

language = "English",

volume = "38",

pages = "126--132",

journal = "Russian Journal of Bioorganic Chemistry",

issn = "1068-1620",

publisher = "МАИК {"}Наука/Интерпериодика{"}",

number = "2",

}

RIS

TY - JOUR

T1 - Identification of rat and human hemoglobin acetylation sites formed as a result of interaction with acetylsalicylic acid

AU - Shreiner, E. V.

AU - Murashko, E. A.

AU - Dubrovskii, Ya A.

AU - Krasnov, N. V.

AU - Podolskaya, E. P.

AU - Babakov, V. N.

PY - 2012/3/1

Y1 - 2012/3/1

N2 - 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.

AB - 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.

KW - Acetylation

KW - Acetylsalicylic acid

KW - Aspirin

KW - Hemoglobin

KW - MALDI-TOF

UR - http://www.scopus.com/inward/record.url?scp=84861124632&partnerID=8YFLogxK

U2 - 10.1134/S1068162012020094

DO - 10.1134/S1068162012020094

M3 - Article

AN - SCOPUS:84861124632

VL - 38

SP - 126

EP - 132

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

SN - 1068-1620

IS - 2

ER -

ID: 36362280