[A method of detecting modifications of tyrosine residues in serum albumin].
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Biomedical subjects
Publications and source records attributed to G V Troitskiĭ.
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Affinity of IgG to the first complement factor C1q was found out to increase in 10-30% glycol solutions. Analytical ultracentrifugation and turbidity data showed that IgG molecules do not aggregate at such concentrations of glycol. The complement-binding effect may be caused by a conformational transition in the IgG molecules.
A modified form of albumin isolated from the blood of oncological patients was studied. A modification of N-terminal amino acid, 50% tyrosine groups, free SH-group of cysteine and lysine group in the fourth position in the N-terminal sequence of amino acids was discovered. The possibility of a post-translation modification of serum albumin in disease in individual amino acid groups is discussed.
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. Although being nonspecific, changes in the extent of despiralization vary depending on tumor advancement and gravity of patient's condition. The level of modified serum albumin is also in correlation with tumor process and the patient's state, the highest values being registered at later stages of the disease.
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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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