Publications by authors named "Bagdasar'ian S"

The frequency of diagnostic errors in examination of 3827 patients with gynecological cancer diseases accounted for 21.6 up to 35%. The conformation of serum albumin in these patients was studied by means of different biochemical assays.

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The temperature-perturbation difference spectra (TPDS) of human serum albumin (NSA) were studied after incubation with different synthetic detergents--anionic, cationic, amphoteric, nonionogenic--in various molar ratios. It is shown that the detergents studied have a different effect on the perturbation of tyrosine residua spectra. Under these conditions the rigidity of their environment depending on the nature and concentration of the mentioned detergents is supposed to change.

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The frequency and causes of diagnostic errors are discussed on the basis of 2,099 case histories of ovarian and uterine tumors. The use of physico-chemical characteristics of serum albumin as an additional means of diagnosis of these diseases in 16 patients and 20 healthy subjects was studied. Patients revealed changes in dispersion of optical rotation of serum albumin which suggest its despiralization.

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The level of blood albumin fucose in healthy subjects and cases of non-tumor pathology and benign tumors of the uterus and ovaries was found to be I nmol of fucose/10 nmol of human serum albumin or lower, whereas in patients with malignant tumors of different localizations it was 4-7 times as high. The highest levels were recorded in patients with primary hepatic cancer and hepatic metastases. The test may be used in differential diagnosis of tumor lesions of different localization as well as for assessment of tumor progression.

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Physicochemical properties of blood serum albumin were studied in sportsmen during physical exercises. The "carbohydrate and lipid capacity' of blood serum albumin is found to increase under physical loads. Albumin is supposed to incorporate more actively into the transport of carbohydrates or lipids used as source of energy in the muscular work.

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Amino acidic composition, dispersion of optic rotation, differential temperature-perturbation spectra, molecular weight and terminal amino acids are studied for certain isoelectric fractions of human serum albumin obtained by means of isoelectric focusing in the borate-polyol system. The isolated three isoelectric fractions with pI 4.7, 4.

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Albumin from blood serum of healthy persons and from patients with various pathologies and different severity of diseases was characterized using isoelectric focusing in borate-polyol system. In all the pathologies studied a new component occurred, which had an isoelectric point at pH 5.5 and which was not found in fresh albumin preparations isolated from healthy persons.

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The method of residementation with trichloracetic acid followed by dissolution in ethanol of preparations of the human serum albumin with changed conformation under conditions of pathology was suggested for determining the amount of modified albumin. The conformationally changed albumin is separated by the mentioned method and it changes to the insoluble form. According to the content of albumin in the sediment it is possible to estimate the amount of the modified part of this protein which was determined previously by the labour-consuming method of optical rotation dispersion.

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Accessibility of tyrosiles in serum albumin of healthy rabbits and those with experimental fatty degeneration of the liver was studied by the termal parturbation spectroscopy. The method determined about 50% of perturbed tyrosiles in albumin of healthy rabbits. Serum albumin of rabbits with fatty degeneration of the liver perturbed 30% of tyrosiles, that evidences for conformational transformations of the rabbit albumin in this pathology.

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The authors studied the optic rotation dispersion of serum albumin in patients suffering from cholecystitis and acute appendicitis. Conforming changes in these forms of pathology characterized by despiralization processes were established. A method of purification of albumin from its modified forms, possibly causing the mentioned changes in the albumin structure is suggested.

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