[The etiological and pathogenetic bases of nephrolithiasis].

A new outlook on etiology and pathogenesis of nephrolithiasis regards renal tubular acidosis (RTA) as the basic pathogenetic factor of nephrolithiasis. These conclusions were made basing on the findings on blood and urine glycolysis enzymes, lactic acid, acid-base metabolism, titrated acids, ammonium. RTA stages responsible for the variety of the forming concrement and two groups of nephrolithiasis etiological factors (acting on epithelial cell of the nephron and involved in urinary processes) are distinguished.

[The nature of the homeostatic changes in nephrolithiasis patients].

Rheorenographic findings, activities of 4 major glycolytic enzymes and 3 Krebs cycle ones in serum and blood, urinary fibrinolytic activity were analyzed in 117 patients with coral nephrolithiasis (the pelvis was drained after calculus removal) in 114 patients with non-coral calculi (the pelvis was sutured) before and 7, 14 days after surgery. Rheography revealed a significant decrease in arterial vascular tone and blood filling and an impairment in venous return in the diseased kidney. In the patients with nephrolithiasis, the enzymatic activity showed 3.

[Results of radionuclide study of the single kidney remaining after nephrectomy in nephrolithiasis].

Computerized dynamic gamma scintigraphy with indirect radionuclide angiography was carried out in 29 patients with a single kidney. It was found that patients with a single kidney show already at the stage of "intact" organ persistent disorders of intrarenal hemodynamic processes as well as chronic urostasis. This variant of radionuclide examination may be used in the prophylactic management of this category of patients.

[Regulatory region of fr phage replicase cistron. II. Isolation and structure of specific fr RNA fragments].

A new set of short RNA templates has been prepared for functional studies in initiation of translation in vitro. Number of individual RNA fragments which contain complete or part of the initiatory region of phage fr replicase cistron were isolated from complex fr RNA--fr coat protein. Their primary structure were determined by using standard fingerprint technique and rapid gel sequencing.