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Bruno Bragança,Maria Trêpa,Raquel Santos,Inês Silveira,Marta Fontes Oliveira,Maria João Sousa,Hipólito Reis,Severo Torres,Mário Santos 한국심초음파학회 2020 Journal of Cardiovascular Imaging (J Cardiovasc Im Vol.28 No.2
BACKGROUND: Right ventriculo-arterial coupling (RV-PA) can be estimated by echocardiography using the ratio between tricuspid annular plane systolic excursion (TAPSE) and pulmonary artery systolic pressure (PASP) and it has prognostic value in the general heart failure (HF) population. We aimed to study the clinical correlates and prognostic value of RV-PA in HF patients undergoing cardiac resynchronization therapy (CRT). METHODS: We retrospectively studied 70 HF patients undergoing CRT implantation. RESULTS: RV-PA coupling was estimated by TAPSE/PASP ratio using baseline echocardiography. Non-response to CRT was defined as improvement of left ventricular ejection fraction < 5% in a follow-up echo 6-12 months after CRT. Those with lower TAPSE/PASP ratios (worse RV-PA coupling) had higher NT-proBNP concentrations and increased E/e′ ratio. TAPSE/PASP ratio and PASP, but not TAPSE, predicted nonresponse to CRT with TAPSE/PASP ratio showing the best discriminative ability with a sensitivity of 76% and specificity of 71%. Among these parameters, PASP independently predicted all-cause mortality. CONCLUSIONS: RV-PA coupling estimated by TAPSE/PASP ratio was associated with established prognostic markers in HF. It numerically outperformed PASP and TAPSE in predicting the response to CRT. Our data suggest that this simple and widely available echocardiographic parameter conveys significant pathophysiological and prognostic meaning in HF patients undergoing CRT.
Chymotrypsin - Eudragit Complex Formation
Valeria Boeris,Laura Verónica Cappella,Gisele Peres,Inés Burgos,Nádya Pesce da Silveira,Gerardo Fidelio,Guillermo Picó 한국생물공학회 2013 Biotechnology and Bioprocess Engineering Vol.18 No.3
Eudragit® L100 (EuL) and Eudragit® S100(EuS) are synthetic polyanions differing on their electric charge density. They interact with chymotrypsin (ChTRP),a basic protein forming soluble and non-soluble complexes. The complex formation was studied by dynamic light scattering, isothermal titration calorimetry, native fluorescence emission, circular dichroism and thermodynamical thermal stability of the enzyme. EuS was able to bind 33 ChTRP molecules while EuL, 60. The binding of ChTRP to both Eu was slightly endothermic and the entropic factor was responsible for the soluble complexes formation. The ChTRP-Eu size increases with pH and the binding of ChTRP to Eu modifies the Eu hydrodynamic radium. The interaction of ChTRP with Eu did not modify its secondary or tertiary structure. The thermal stability of ChTRP was increased when it interacted with both Eu.