[Identification of rat and human hemoglobin acetilation sites after its interaction with acetylsalicylic acid].
The possibility of interaction of 0.1 mg/mL acetylsalicylic acid with purified human and rat globin in vitro during 24 h at 37 degrees C was investigated. The rat globin can be modified with acetylsalicylic acid on aminoacid residues K-17, K-57, K-91, K-140 in alpha subunit as well as on K-18, K-77 in beta subunit. The human globin can be modified with acetylsalicylic acid on aminoacid residues K-17, K-41, K-57 and K-91 in alpha subunit as well as on K-18, K-96 and K- 133 in beta subunit. We identified of acetetylated lysines K-17 and K-57 in alpha subunit of human hemoglobin after incubation whole blood with 0.1 mg/mL acetylsalicylic acid during 3 h.
E V
EV
Shreĭner
E A
EA
Murashko
Ia D
IaD
Dubrovskiĭ
N V
NV
Krasnov
E P
EP
Podol'skaia
V N
VN
Babakov
D000107:Acetylation; D000818:Animals; D001241:Aspirin / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D051381:Rats; D013997:Time Factors
D006454:Hemoglobins; D001241:Aspirin