Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Carmela M. A. Barone"'
Autor:
Antonio Palladino, Elena De Felice, Chiara Attanasio, Carmela M. A. Barone, Antonio Crasto, Livia D’Angelo, Daniela Giaquinto, Claudia Lambiase, Paola Scocco, Francesco Serrapica, Lucianna Maruccio
Publikováno v:
Animals, Vol 13, Iss 3, p 420 (2023)
Among the most-used fish species in aquaculture is the Nile tilapia, due to its rapid growth rate and its adaptation to a wide range of farming conditions. A careful description of the morphology of the digestive tract, particularly the esophagus and
Externí odkaz:
https://doaj.org/article/7389075b5d684b09b0634e1393ed5efd
Autor:
Roberta Cimmino, Carmela M. A. Barone, Salvatore Claps, Ettore Varricchio, Domenico Rufrano, Mariangela Caroprese, Marzia Albenzio, Pasquale De Palo, Giuseppe Campanile, Gianluca Neglia
Publikováno v:
BMC Veterinary Research, Vol 14, Iss 1, Pp 1-11 (2018)
Abstract Background Diet supplementation with polyphenols is a novel strategy to improve meat quality in livestock, by preventing oxidative deterioration of lipids and protein. Polyphenols have beneficial effects on both human and animal health and c
Externí odkaz:
https://doaj.org/article/cbcab5ee075a49f797ef931ee497e970
Autor:
Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Vincenzo Carginale, Giovanni Sansone, Carmela M. A. Barone, Mosè Rossi, Fatmah A. S. Alasmary, Sameh M. Osman, Zeid AlOthman, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 1029-1035 (2017)
We cloned, expressed, purified, and determined the kinetic constants of the recombinant α-carbonic anhydrase (rec-MgaCA) identified in the mantle tissue of the bivalve Mediterranean mussel, Mytilus galloprovincialis. In metazoans, the α-CA family i
Externí odkaz:
https://doaj.org/article/fff9f1a1da964a998d406da9e156831c
Autor:
Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Giovanni Sansone, Carmela M. A. Barone, Mosè Rossi, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Marine Drugs, Vol 15, Iss 9, p 270 (2017)
The carbonic anhydrase (CA, EC 4.2.1.1) superfamily of metalloenzymes catalyzes the hydration of carbon dioxide to bicarbonate and protons. The catalytically active form of these enzymes incorporates a metal hydroxide derivative, the formation of whi
Externí odkaz:
https://doaj.org/article/985079a6e0d340f48a3edc69a93a91df
