[The pathochemical characteristics of oligomeric forms of Tamm-Horsfall protein under urolithiasis]

The role of Tamm-Horsfall protein in pathogenesis of urolithiasis was analyzed. The study of oligomeric forms of protein was carried out using technique of dynamic light scattering. The sampling of 57 patients with urolithiasis and 51 patients of control group of comparative age and gender were examined. The degree of purification of Tamm-Horsfall protein was controlled using denaturant electrophoresis in polyacridine amyl gel. The reversing change of oligomeric form of protein with molecule size 2 Mda in polymeric form 28 Mda under impact of guanidinhydrochloride. Under urolithiasis, the form of protein associated with non-organic components and with size of macromolecular complex larger than 1500 nm was detected. The diagnostic criterion of urolithiasis was proposed based on totality of biochemical and biophysical analyses of urine.