RESUMEN
Comparison of acute pain syndrome after septoplasty, rhinoplasty, and rhinoseptoplasty was carried out. It is shown that the intensity of acute pain is higher in patients after rhinoseptoplasty in the first 3-6 h after surgery.
Asunto(s)
Dolor Agudo , Rinoplastia , Humanos , Rinoplastia/efectos adversos , Cavidad Nasal/cirugía , Tabique Nasal/cirugía , Dolor Agudo/etiología , Dolor Agudo/cirugía , Resultado del TratamientoRESUMEN
Dipeptidyl peptidase II (DPPII) from bovine kidney cortex and lung was purified to the electrophoretically homogeneous state. The molecular and catalytic characteristics of the enzyme were determined. It was revealed that DPPII preparations possess adenosine deaminase (ADA) activity at all purification steps. For the first time, the ADA-binding ability of DPPII has been shown similar to the well-known ADA-binding enzyme, DPPIV. The dissociation constant of the DPPII-ADA complex was estimated using a resonant mirror biosensor (80 nM), fluorescence polarization (60 nM), and differential spectroscopy (36 nM) techniques. The data demonstrate that DPPII can form a complex with ADA, but with one order of magnitude higher dissociation constant than that of DPPIV (7.8 nM).
Asunto(s)
Adenosina Desaminasa/metabolismo , Dipeptidil-Peptidasas y Tripeptidil-Peptidasas/metabolismo , Complejos Multiproteicos/metabolismo , Adenosina Desaminasa/aislamiento & purificación , Animales , Bovinos , Dipeptidil Peptidasa 4/metabolismo , Dipeptidil-Peptidasas y Tripeptidil-Peptidasas/aislamiento & purificación , Humanos , Corteza Renal/enzimología , Pulmón/enzimología , Unión ProteicaRESUMEN
The interaction of adenosine deaminase (adenosine aminohydrolase, ADA) from bovine spleen with inhibitors--erythro-9-(2-hydroxy-3-nonyl)adenine, erythro-9-(2-hydroxy-3-nonyl)-3-deazaadenine, and 1-deazaadenosine--was investigated. Using selective chemical modification by diethyl pyrocarbonate (DEP), the possible involvement of His residues in this interaction was studied. The graphical method of Tsou indicates that of six His residues modified in the presence of DEP, only one is essential for ADA activity. Inactivation of the enzyme, though with low rate, in complex with any of the inhibitors suggests that the adenine moiety of the inhibitors (and consequently, of the substrate) does not bind with the essential His to prevent its modification. The absence of noticeable changes in the dissociation constants of any of the enzyme-inhibitor complexes for the DEP-modified and control enzyme indicates that at least the most available His residues modified in our experiments do not participate in binding the inhibitors--derivatives of adenosine or erythro-9-(2-hydroxy-3-nonyl)adenine.