[Polyfunctional inhibitors of proteolytic enzymes in the therapy of patients with chronic purulent maxillary sinusitis]. / Primenenie polifunktsional'nykh ingibitorov proteoliticheskikh fermentov v lechenii bol'nykh khronicheskim gnoinym gaimoritom.

Using clinical and biochemical data, the efficacy of the topical application of kontrikal, a polyfunctional inhibitor of proteinases, for the therapy of chronic purulent sinusitis is discussed. The drug was found to reduce the activity of proteolytic enzymes in the purulent exudate from the maxillary sinus. As compared with the controls (27 patients), the treated group (38 patients) showed a rapid disappearance of clinical manifestations, shortening of the therapeutic period, increase of proteinase inhibitors and decrease of protein in the exudate.

[Study of proteolytic enzymes and their inhibitors in maxillary sinus exudates in patients with chronic suppurative maxillary sinusitis]. / Issledovanie proteoliticheskikh fermentov i ikh ingibitorov v ékssudatakh verkhnecheliustnykh pazukh bol'nykh khronicheskim gnoinym gaimoritom.

Specific proteolytic and antitryptic activities were measured in the sinus exudate of 27 patients with chronic suppurative maxillary sinusitis. Most patients showed a shift in the proteinase-inhibitor system with proteolytic activity being predominant. In the course of treatment antitryptic activity in the exudate increased. It was found that biochemical data were correlated with clinical manifestations. It is concluded that patients with the above pathology should be prescribed proteolytic enzymes on an individual basis and that natural proteinase inhibitors should be included into the combined therapy.

[Effect of proteolytic inhibitors from human plasma on the activity of native and immobilized terrilytin]. / Vliianie proteoliticheskikh ingibitorov plazmy krovi cheloveka na aktivnost' nativnogo i immobilizirovannogo terrilitina.

Human blood plasma inhibitors are studied for their effect on the activity of terrilytin, a proteolytic enzyme of microbial origin, and terridecase, its immobilized form. The main plasma inhibitor of terrilytin is alpha 2-macroglobulin (alpha 2 MG). The pattern of terrilytin and terridecase interaction with alpha 2 MG preparation isolated from human blood plasma has also been studied. The inhibitor is found to exert a slight retarding effect on the terridecase activity. Significant differences in alpha 2 MG inactivation of terrilytin and trypsin are observed.