Biomedical subjects

V S Koniaeva

Publications and source records attributed to V S Koniaeva.

4 recordsLinked to original sources

PubMedDate not supplied

[Study of hemoglobin structure by a turbidimetric method].

The initial velocity of coagulation of human oxyhemoglobin in tris-HCl buffer measured by turbidimetric method, pH 7.2 in the presence of phenylmercuryacetate made it possible to estimate the amount of moles of this reagent stechiometrically binding with hemoglobin without coagulation of the latter. At 15-30 degrees C this amount is 30-34 mole per hemoglobin-tetramer. At temperature increase from 30 to 42.5 degrees C the amount of the reagent necessary for protein coagulation sharply decreases. A model is proposed assuming that oxyhemoglobin coagulation proceeds only during binding of the reagent with specific protein sites.

Hemoglobins↗

PubMedDate not supplied

[Effect of phenylmercury derivatives on human oxyhemoglobin].

By the dynamics of human oxyhemoglobin coagulation in the presence of phenyl mercury acetate in tris-AcOH buffer, pH 7.2 the number of moles of PhHg+ stechiometrically bound with protein at different temperatures was estimated. Within the temperature range 15-30 degrees C this value is constant--32-34 mole per 1 mole of HBO2-tetramer. Within the range 30-40 degrees C it rises to approximately 40. Coagulation of oxyhemoglobin modified with PhHg+ cation is reversible in contrast to HBO2 coagulation modified with uncharged PhHgCl.

Humans↗

PubMedDate not supplied

[Migration of parachloromercuribenzoic acid along the binding sites of hunan oxyhemoglobin].

Oxidation kinetics-characterized state of human oxyhemoglobin bound with p-chloromercuribenzoic acid (PCMB) (above 2 mole per tetramer) is changed during incubation at 20 degrees C. This suggests transfer of PCMB molecules from primary occupied centres to the secondary ones having higher affinity to PCMB. The same effect is observed at increased temperature without incubation. By means of gel-chromatography the hypothesis that the change of oxyhemoglobin state is accompanied by its increased equilibrium dissociation into dimers is acknowledge.

Binding Sites↗

PubMedDate not supplied

[Specific interaction of piperidine derivatives with human serum albumin].

When the series of 4-substituted derivatives of 2,2,6,6-tetramethyl piperidine-I-oxide (TMPO) interacts with human serum albumin (HSA) in 0.01 M Na-acetate buffer, pH 5.6 in differential spectra there appears the intensive maximum at 232-235 nm characteristic of protein denaturation. It is suggested that specifics of nitroxyl binding with HSA is mainly determined by the conformational state of TMPO (twist or chair), since corresponding 4-nitro piperidines having other conformation result in the appearance of the band at 232.5 nm with a much lower intensity. It is recommended to take into account possible significant structural changes of albumins when studied by the spin label method using TMPO or its derivatives.

Humans↗