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Biomedical subjects

K F Selivanova

Publications and source records attributed to K F Selivanova.

At least 19 recordsLinked to original sources
PubMed1990

[Hemodynamic changes in patients with bronchial asthma].

Examined were 140 patients with bronchial asthma (stage I). The state of hemodynamics was influenced by several factors--duration and gravity of the disease, frequency of exacerbations, severity of organic changes of the bronchopulmonary apparatus. The hyperkinetic type of circulation was observed mainly in mild course of the disease and on early stages of bronchial asthma. As the organic changes in the lung and myocardium increase the number of cases with hypokinetic type of circulation rises.

Asthma↗
PubMed1989

[Glycosylated hemoglobin (HbA1c) in blood in impaired tolerance to glucose and sugar diabetes].

Isoelectric focussing in borate-poliol system is employed for measuring the blood glycosylated hemoglobin (HbA1c) levels at the treatment and prophylaxis institutions in Yalta. Examinations of normal subjects and patients with disordered glucose tolerance and apparent diabetes mellitus have revealed a significant elevation of HbA1c level in the patients with impaired glucose tolerance vs. normal subjects; these levels have been virtually the same in the diabetics and patients with impaired glucose tolerance. Over the course of health resort treatment the diabetics develop negligible changes in the HbA1c levels, paralleled by a significant reduction of glycemia on an empty stomach.

Diabetes Mellitus↗
PubMedDate not supplied

[Study of peptide composition in serum albumin in patients with thyroid gland dysfunction].

Trypsin hydrolyzates of blood serum albumin of healthy people and patients with diffuse thyrotoxicosis and hypothyreosis were studied by the cellulose thin-layer electrochromatography. All the patients were found to have changes in the peptide composition of albumin trypsin hydrolyzate which resulted in disappearance of some peptides as well as in the appearance of new ones. Simultaneously conducted measurements of dispersion of optical rotation detected some changes in spectropolarimetric characteristics which provide the evidence for disperalization of its molecule. The found changes in albumin are determined by the disorder of normal protein biosynthesis and possible metabolic damage of protein.

Humans↗
PubMedDate not supplied

[Level of hemoglobin A1c and modified blood serum albumin in patients with diabetes mellitus].

Hemoglobin A1c was studied by means of isoelectric focusing in borate-polyol system and modified albumin--using electrophoresis of blood serum on acetate-cellulose films with subsequent TCA-ethanol sedimentation in healthy volunteers and patients with diabetes mellitus. These parameters were increased in the patients, whereas content of the albumin was decreased and the content of hemoglobin A1c was altered only slightly during treatment of diabetes. Content of hemoglobin A1c and modified albumin was shown to depend on the compensation state of diabetes mellitus.

Blood Glucose↗
PubMedDate not supplied

[Subfractional composition and structural characteristics of G immunoglobulins in pathological states].

Physico-chemical properties of gamma-globulin fraction and immunoglobulins G (IgG) were studied, using temperature-perturbational differential spectrophotometry and ion exchange chromatography on DEAE cellulose, in blood serum of 118 patients with impairments of thyroid gland and of 28 patients with chronic pneumonia. Amount of tyrosine residues, perturbated by temperature, was decreased and an alkaline subfraction was increased in IgG of patients with toxic goiter and chronic pneumonia; the increase in the alkaline subfraction was more distinct in impairments of thyroid gland. The data obtained suggest that the alkaline subfraction is characterized by an increased rigidity and apparently by altered structural properties in toxic goiter. The tyrosine residues in IgG enable to evaluate effectively the availability of a cavity between variable domains (antigen-antibody site) of the immunoglobulin.

Adult↗