[Study of serum protein aggregation after treatment with urea].
Gel chromatography and electrophoresis in polyacrylamide gel show that urea in vitro induces aggregation of blood proteins, with their content unchanged. The aggregation does not depend on the fibrinogen available. Comparison of the data on the effect of urea, DS-Na and thermal denaturation on the protein aggregation suggests that the aggregation is induced by local conformation transformations in the structure of certain protein molecules. At the same time, the data obtained do not permit neglecting the role of denaturation in the aggregation.
D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008074:Lipoproteins / Q000032:analysis; D011487:Protein Conformation / Q000187:drug effects; D051381:Rats; D012709:Serum Albumin / Q000032:analysis; D014508:Urea / Q000494:pharmacology*
D001798:Blood Proteins; D008074:Lipoproteins; D012709:Serum Albumin; D014508:Urea
Issledovanie agregatsii belkov syvorotki krovi pod vliianiem mocheviny.