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Biomedical subjects

A P Levitskiĭ

Publications and source records attributed to A P Levitskiĭ.

At least 19 recordsLinked to original sources

[Soybean bacteriological culture media and prospects for their use in clinical bacteriology].

Agar bacteriological nutrient media are suggested, based on soybean extract subjected to enzymatic hydrolysis and lyophilized native. The growth of test strains, number of grown colonies and their size were virtually the same as after inoculation of these strains in control nutrient media. Soybean salt medium with yolk suspension was tried with good results as elective medium for isolation of staphylococci from clinical material. Commercial manufacture of these media mainly from native soybean extract is proposed.

Bacteriological Techniques↗

[The use of protease inhibitors in the treatment of burn wounds].

The results of experimental and clinical studies of the effect of contrykal and aminocaproic acid on tissue regeneration in deep burns are presented. In the experiment, by means of planimetric, histologic, histochemical and biochemical methods of investigation, the positive effect of inhibitors on healing of the burn wounds is shown. In treatment of 272 patients with deep burns, it was established that use of protease inhibitors at the phase of regeneration contributed to 2-fold acceleration of marginal epithelization, shortening of time of would preparation to autodermoplasty by 3-4 days, increase in effectiveness of survival of the cutaneous flaps. A possibility of wide clinical use of proteolysis inhibitors predominantly in combination with antibiotics is shown.

Animals↗

[Clinico-enzymologic parallels in patients of reproductive age with benign epithelial ovarian tumors].

Proteolytic enzymes and their inhibitors have been assayed in sera of 120 patients with benign epithelial ovarian tumors during preoperative menstrual cycles and in 3 years following surgery. The patients showed imbalances in protease inhibitors which failed to be improved by the operative treatment in a proportion of patients. Follow-up of this patient population is recommendable. A serum elastase test was proposed to predict benign epithelial ovarian tumors.

Adult↗

[Use of epsilon-aminocaproic acid for treating granulating burn wounds].

Results of the application of synthetic inhibitor of proteolytic enzymes epsilon-aminocaproic acid in the treatment of granulating burn wounds are described. High effectiveness of the aminocaproic acid in healing of granulating wounds after burns is shown as well as in preparing great granulating burn wounds for autodermoplasty and the take of transplanted autodermic flaps.

Adolescent↗

[Effect of kallikrein and its inhibitor on absorption from the abdominal cavity in peritonitis].

Experiments were carried out in 195 albino rats. It was established that in acute peritonitis the rate of absorption of the colloid dye (tryptan blue) was sharply decreased. Kallikrein somewhat increased the absorption rate, especially at early terms while the inhibitor (kontrikal) was shown to substantially decrease it. The mode of injection (intravenous or intraperitoneal) failed to influence manifestations of the biological effect of the drug. The data obtained show that a disturbed absorption from the abdominal cavity may be corrected in acute peritonitis by injections of kallikrein.

Abdomen↗

[Changes in the serum acid phosphatase activity of guinea pigs poisoned with C1 perfringens type A toxin and a mixture of toxin and a broth culture filtrate].

It was shown in experiments on guinea pigs that the injection of C1. perfringens type A toxoid induced an increase in acid phosphatase activity of animal blood serum. The action of the toxoid increased under the effect of C1. butyricum cultural filtrate, which gave rise to an earlier enhancement of the specific activity of the enzyme as compared to the injection of the toxoid alone. Increased activity of acid phosphatase may play a pathogenetic role in cases of anaerobic infection caused by association of C1. perfringens and C1. butyricum.

Acid Phosphatase↗