L. R. Gudkin

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Lyophilized polymerized hemoglobin has no group specificity and does not damage the kidney after 2 days of storage; its T/2 is 14-16 hours. P50 of solution prepared on the hemoglobin basis is 24-28 torr at 37 degrees C and pCO2, 40 torr in 0.05 M Tris-buffer, pH 7.4. As was shown in models of hemorrhagic shock in dogs, the hemodynamic properties of the(More)
Electrochemical properties of macromolecules of modified haemoglobin obtained by polycondensation with glutaric aldehyde have been investigated by means of potentiometric titration, PAG-electrophoresis, ion-exchange chromatography, and (for evaluation of isoelectric point) distribution between two aqueous polymeric phases. Introduction of additional(More)
Solutions of oligohemoglobins (OHb) with middle molecular mass 100 x 10(3) = 400 x 10(3), obtained after polycondensation of hemoglobin with glutaric aldehyde as well as oligohemoglobin modified with pyridoxal-5-phosphate, were studied in vivo and in vitro (plethoric administration, isovolemic metabolic substitution, hemorrhagic shock; at a dose of 0.5-1.8(More)
Polymer aspects of polycondensation of pyridoxylated hemoglobin with glutaraldehyde have been considered. On the basis of the investigation of reaction kinetics, the mechanism of chemical crosslinking of hemoglobin molecules into oligohemoglobin is proposed. Owing to the statistical character of the reaction, the resulting macromolecules are polydisperse(More)
Polycondensation of a catalase (EC 1.11.1.6) with glutaraldehyde in order to stabilize the quaternary structure of an enzyme, maintain its activity, and protect it from thermal denaturation was studied. Synthesis showed a superequivalent utilization of the aldehyde groups relative to the catalase amine groups, as a result of the formation of glutaraldehyde(More)
The process of association-dissociation of hemoglobin molecules into dimers of its subunits in water and water-saline solutions is studied by the method of gel-penetrating chromatography and ultrafiltration. The quantitative assessment of stabilization of quaternary structure of hemoglobin in chemically bound polymer derivative in comparison with native(More)
Development of a plasma expander and oxygen carrier based on hemoglobin is an urgent problem in modern transfusiology. The use of solutions of native hemoglobin is made difficult by its rapid excretion from the blood stream, its high affinity for oxygen, and its unfavorable action on function of the kidneys, liver, and other organs [i, 4, 5, 15].(More)
Oligomeric hemoglobins were produced after polycondensation with glutaric aldehyde (OHb) as well as after modification with pyridoxal-5-phosphate (OHb-PLP). OHb exhibited high affinity to oxygen (P50 = 17 torr) as well as a decreased rate of the subunits cooperative interaction (n = 1.5-1.6); OHb-PLP possessed P50 = 27 torr, n = 2.2 (for pO2 greater than(More)