Role of Purinergic Receptors of Erythrocytes in the Regulation of Conformation and Oxygen- and NO-Transporting Capacity of Hemoglobin.

Raman spectroscopy was used to investigate changes in hemoglobin conformation and its ability to transfer O2 and NO induced by activation of purinergic receptors of erythrocytes with extracellular ATP. It was found that addition of ATP in a final concentration of 0.1 mM and higher to erythrocyte suspension was followed by changes in hematoporphyrin conformation, while addition of ATP in a concentration of 1 mM and higher increased the proportion of oxyhemoglobin and NO-associated hemoglobin complexes. In case of purinergic receptors activation in blood erythrocytes, significant changes in hemoglobin conformation were observed only at a final ATP concentration of 5 mM, probably due to buffer properties of the blood.

[Insulin-like growth factor 1-induced changes in hemoporphyrin conformation in hemoglobin and NO-transporting function in human erythrocytes].

The evidence on the effect of different insulin-like growth factor concentrations on a state of human erythrocytes is provided. Activation of the insulin-like growth factor receptors led to changes in the conformation of hemoglobin, NO-transporting function in erythrocytes and also in micro-viscosity of the cell membrane. It was shown for the first time that at the binding of the insulin-like growth factor to a cell surface, hemoglobin of erythrocytes alters its conformations and affinity to ligands.

1-(8-Bromo-2-methyl-4-thioxo-3,4,5,6-tetra-hydro-2H-2,6-methano-1,3-benzoxazocin-11-yl)ethanone.

In the title compound, C(14)H(14)BrNO(2)S, there are two similar non-equivalent mol-ecules in the asymmetric unit, displaying three chiral centres each. In the crystal structure, they are linked by inter-molecular N-H⋯O hydrogen bonds to form infinite chains, which are in turn connected by weak Br⋯H and S⋯H inter-actions.