title: [The action of regulator peptides with different biological activities on the process of fibrin-monomer polymerization and on nonenzymatic fibrinolysis].
abstract: It is shown that preparations of regulatory peptides (RP): interleukin-1, thymoptin, and the endogenous nonpeptide opioid salsalinol produce a marked depolymerization effect on the fibrin-monomer and display nonenzymatic fibrinolytic activity in relation to unstabilized fibrin. Preparations of regulatory peptides thymalin and diphensin of rabbits intensify fibrin polymerization. A single intravenous infusion of diphensin preparation inhibits nonenzymatic fibrinolysis of blood plasma in vivo and in vitro. Repeated intramuscular injections of the immunoactive preparation thymoptin intensify the fibrinolytic properties of blood plasma in rats.
authors.forename: I P
authors.initials: IP
authors.lastname: Ashmarin
authors.forename: L A
authors.initials: LA
authors.lastname: Liapina
authors.forename: V E
authors.initials: VE
authors.lastname: Pastorova
authors.forename: B A
authors.initials: BA
authors.lastname: Kudriashov
mesh_terms: D000818:Animals; D004723:Endorphins / Q000494:pharmacology; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis / Q000187:drug effects*; D005340:Fibrinogen / Q000032:analysis / Q000187:drug effects; D005342:Fibrinolysis / Q000187:drug effects*; D006487:Hemostasis / Q000187:drug effects; D006801:Humans; D066298:In Vitro Techniques; D010455:Peptides / Q000494:pharmacology*; D011817:Rabbits; D051381:Rats; D013997:Time Factors
chemical_list: D004723:Endorphins; D005338:Fibrin Fibrinogen Degradation Products; D010455:Peptides; C011468:fibrinmonomer; D005340:Fibrinogen
vernacular_title: Deĭstvie reguliatornykh peptidov s razlichnoĭ biologicheskoĭ aktivnost'iu na protsess polimerizatsii fibrin-monomera i nefermenttativnyĭ fibrinoliz.