Application of lanthanum stearate monolayers as a metal-affinity sorbent for the selective sorption of soman adducts to human serum albumin.

A new metal-affinity sorbent based on lanthanum stearate monolayers has been developed and characterized. The prospect of its application to specific extraction of organophosphorous compound (OP) adducts of blood proteins was demonstrated. For this, the patterns of soman adducts of human serum albumin (HSA) were comprehensively characterized by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF-MS).

[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.