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| Cheret, Romuald; Delbarre Ladrat, Christine; De Lamballerie Anton, Marie; Verrez-bagnis, Veronique. |
| Post mortem tenderization is one of the most unfavourable quality changes in fish muscle and this contrasts with muscle of mammalian meats. The tenderization can be partly attributed to the acid lysosomal cathepsins and cytosolic neutral calcium-activated calpains. In this study, these proteases from fish and bovine muscles were quantified and compared. The cathepsin B and L activities were in more important amounts in sea bass white muscle than in bovine muscle. On the other hand, cathepsin D activity was 1.4 times higher in meat that in fish muscle, while cathepsin H was negligible in both muscles. Calpain activities were similar in both types of muscle. Moreover, calpastatin (calpain endogenous inhibitor) level is 3.9 times higher in sea bass white... |
| Tipo: Text |
Palavras-chave: Meat; Fish; Protease; Cathepsin; Calpain. |
| Ano: 2007 |
URL: http://archimer.ifremer.fr/doc/2007/publication-3646.pdf |
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| Sciani,Juliana Mozer; Antoniazzi,Marta Maria; Neves,Adriana da Costa; Pimenta,Daniel Carvalho. |
| Background Echinometra lucunter is a common American sea urchin responsible for the majority of the marine accidents in Brazil. Although not lethal, these accidents are reported to be extremely painful. Recently, our group described the presence of toxins in its spines that contribute to the pathological reactions. Additionally, we have observed that the E. lucunter spines can regenerate when broken. In the present work we evaluated the enzymatic activities of sea urchin spine extracts in order to identify an enzyme that could contribute not only to the toxicity, but also participate in the spine growth and regeneration. Results The spine aqueous extract was tested for peptidase activity, with synthetic substrates, in the presence and absence of inhibitors... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Echinometra lucunter; Spines; Cathepsin; Proteolysis. |
| Ano: 2013 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100318 |
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| Peres,G.B.; Juliano,M.A.; Aguiar,J.A.K.; Michelacci,Y.M.. |
| It has been previously shown that dextran sulfate administered to diabetic rats accumulates in the liver and kidney, and this could be due to a malfunction of the lysosomal digestive pathway. The aim of the present study was to evaluate the expression and activities of lysosomal enzymes that act upon proteins and sulfated polysaccharides in the livers of diabetic rats. Diabetes mellitus was induced by streptozotocin in 26 male Wistar rats (12 weeks old), while 26 age-matched controls received only vehicle. The livers were removed on either the 10th or the 30th day of the disease, weighed, and used to evaluate the activity, expression, and localization of lysosomal enzymes. A 50-60% decrease in the specific activities of cysteine proteases, especially... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Liver; Diabetes mellitus; Lysosomal enzymes; Cathepsin; Glycosidase; Sulfatase. |
| Ano: 2014 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2014000600452 |
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