Download full-text PDF |
Source |
---|
Zh Mikrobiol Epidemiol Immunobiol
November 2001
State Medical University, Kursk, State Medical University, Moscow, Russia.
The impact of proteolytic enzymes on the humoral immune response, survival rate and mean survival time of mice, infected with S. aureus culture and receiving antibiotics was studied. Infection with staphylococcal suppressed the formation of antibodies to sheep red blood cells.
View Article and Find Full Text PDFZh Mikrobiol Epidemiol Immunobiol
September 2001
State Medical University, Kursk, Russia.
As revealed in this study, massive burn trauma manifestly suppresses the genesis of antibodies to T-dependent antigen (sheep red blood cells). The administration of ampicillin to the burned animals enhances immunosuppression, while gentamicin produces no essential impact on immune processes under these conditions. Proteolytic enzymes, terrilytin and terridecase, have corrective influence on disturbances in immune response in animals with burns.
View Article and Find Full Text PDFPrikl Biokhim Mikrobiol
November 1997
Joint immobilization of a proteolytic enzyme (terrilytin, protease C, or collytin) and an antimicrobial compound or the bacteriolytic enzyme lysozyme in the structure of polyvinyl alcohol was studied. Changes in the activity of immobilized enzymes upon x-ray sterilization were studied. These materials were highly effective in wound healing.
View Article and Find Full Text PDFAntibiot Khimioter
August 1997
The influence of immobilized proteases such as catalytin (a complex preparation containing the protease terrilytin and the antiseptic catapol) and streptodecase (an activator of fibrinolysis proteases) on the humoral immune response induced by the thymus-dependent antigen (SRBC) under conditions of burns and Staphylococcus infected burns was studied. The immobilized proteases catalytin and streptodecase had an immunostimulating effect under conditions of extended burns. Catalytin had an immunocorrigating effect under conditions of the infected burns.
View Article and Find Full Text PDFProperties of joint immobilization of a proteolytic enzyme (terrilytin, trypsin, collytin, or protease C) and an anti-microbe compound to cellulose copolymer containing carboxyl groups were investigated. It was established that the molecule of anti-microbe substance containing a few base groups enhanced stability of the enzyme immobilized, most likely due to additional fixation of the enzyme macromolecule. Changes in activity of the materials containing both protease and anti-microbe compound were studied upon gamma-sterilization and subsequent prolonged storage.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!