http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8904
Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii (Articolo in rivista)
- Type
- Label
- Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1111/j.1742-4658.2007.06136.x (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Brier S.; Maria G.; Carginale V.; Capasso A.; Wu Y.; Taylor R.M.; Borotto N.B.; Capasso C.; Engen J.R. (literal)
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- NE Univ Boston, Barnett Inst Chem & Biol Anal, Dept Chem & Chem Biol, Boston, MA USA
CNR, Inst Prot Biochem, Naples, Italy (literal)
- Titolo
- Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii (literal)
- Abstract
- The Antarctic notothenioid Trematomus bernacchii (rock cod) lives at a constant mean temperature of -1.9 degrees C. Gastric digestion under these conditions relies on the proteolytic activity of aspartic proteases such as pepsin. To understand the molecular mechanisms of Antarctic fish pepsins, T. bernacchii pepsins A1 and A2 were cloned, overexpressed in Escherichia coli, purified and characterized with a number of biochemical and biophysical methods. The properties of these two Antarctic isoenzymes were compared to those of porcine pepsin and found to be unique in a number of ways. Fish pepsins were found to be more temperature sensitive, generally less active at lower pH and more sensitive to inhibition by pepstatin than their mesophilic counterparts. The specificity of Antarctic fish pepsins was similar but not identical to that of pig pepsin, probably owing to changes in the sequence of fish enzymes near the active site. Gene duplication of Antarctic rock cod pepsins is the likely mechanism for adaptation to the harsh temperature environment in which these enzymes must function. (literal)
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