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Streptozotocin-induced diabetes mellitus affects lysosomal enzymes in rat liver BJMBR
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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Hydrolytic potential of a psychrotrophic Pseudomonas isolated from refrigerated raw milk BJM
Corrêa,Ana Paula F.; Daroit,Daniel J.; Velho,Renata V.; Brandelli,Adriano.
The production of extracellular hydrolases by a psychrotrophic bacterium isolated from refrigerated raw milk, and identified as a Pseudomonas sp. belonging to the Pseudomonas jenssenii group, was studied. This bacterium produced proteolytic and lipolytic enzymes in all media investigated (skim milk, cheese whey, casein broth, and tryptone soy broth). High levels of α-glucosidase were produced in skim milk broth. Hydrolytic enzymes detected in skim milk broth are of particular concern, indicating that these enzymes could be produced by Pseudomonas sp. during the cold storage of raw milk, contributing to the spoilage problem in milk and dairy products.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Pseudomonas; Hydrolases; Protease; Lipase; Glycosidase.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000400034
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