[Indexes of a functional condition of a liver with hemolytic disease of the newborn stipulated incompatibility between the mother and fetus].

The hemolytic disease of the newborn, originating as a result of sensitization of the mother to the Rh-antigen of erythrocytes of the fetus (Rh-HDN) is one of the most important causes of the loss of a fetus and newborn. One of the pathogenetic mechanisms of Rh-HDN is the hyperbilirubinemia at the expense of the toxiferous fraction of a bilirubin negatively influencing many organs of the child, including the liver. The purpose of the work was the complex study of indexes of a functional condition of a liver newborn with a various degree of gravity Rh-HDN and definition of effectiveness of the conducted therapy.

[Accessibility of tryptophan residues in immunoglobulin M molecule as an indicator of its conformational variability].

The accessibility of tryptophan residues in immunoglobulin M to modification with the Koshland reagent (2-hydroxy-5-nitrobenzyl bromide) was used as an indicator of its conformational variability. Of 14 tryptophan residues (per HL-fragment) in the native IgM, only one (presumably Trp312 in the mu-chain) was the most accessible. Irreversible acid- or temperature-induced conformational changes of IgM increased almost 2-fold the number of accessible tryptophan residues.

[Modification of tryptophan residues in immunoglobulin M by 2-hydroxy-5-nitrobenzyl bromide].

The modification of tryptophan residues in monoclonal immunoglobulin M (IgM) by 2-hydroxy-5-nitrobenzyl bromide (RK) was studied at pH 2.0-2.85 and 7.

Some peculiarities of the dynamics of the immunoglobulin M structure.

The isotropic mobility of separate regions of the intact molecule of immunoglobulin M (IgM) and its Fab and (Fc)5 fragments was studied using spin-labeling of carbohydrate (2,2,6,6-tetramethyl-4-aminopiperidine-1-oxyl) and peptide (2,2,5,5-tetramethyl-3-dichlorotriazinylaminopyrrolidine-1-oxyl) moieties. The spin-labeled oligosaccharide groups (OGs) in the Fab region are shown to have much more amplitude of anisotropic motion than those in the (Fc)5 region. The spin label in the latter is evidently attached in the C mu 3 domain to one of its OGs which is probably stabilized by ionic contacts between terminal N-acetylneuraminic acid residue and the peptide moiety of the IgM molecule.