ABSTRACT
Os autores determinaram a capacidade da pentamicina e derivados bis-benzamidinicos em inibir a açao da trombina, estudando os reflexos da mistura destas substancias, com plasmas normais, nos testes laboratoriais de avaliaçao da coagulaçao sanguinea.
Subject(s)
Animals , Rabbits , Rats , Blood Coagulation Tests , Chemistry , Hematologic Tests , In Vitro Techniques , Pentamidine , BrazilABSTRACT
1. The determination of the binding of 4,4'diazoamino-bis-benzamidine (DABB) to alfa-trypsin by equilibrium measurements in columns indicated a stoichiometry of 2 mol ligan/mol enzyme. One molecule binds to the secondy binding site, sith Ki2=mMat pH8,0, 25-C. 2. Bovine pancreatic trypsin inhibitor (BPTI) prevented binding of DABB to both sites, indicating that they are topographically close and within the interface of the trypsin-BPTI complex. 3. On the basis of data from the interface of the trypsin-BPTI complex, we concluded that the secondary binding site of trypsin is plausibly identified as the same site in trypsin that binds the Arg-17 reside of BPTI, i.e., Tyr-39 and Tyr-151 in bovine trypsin. This site would then correspond to subsite S'2 on the enzyme surface