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| da-Silva,A.M.; Zapella,P.D.A.; Andrioli,L.P.M.; Campanhã,R.B.; Fiorini,L.C.; Etchebehere,L.C.; da-Costa-Maia,J.C.; Terenzi,H.F.. |
| Preference for specific protein substrates together with differential sensitivity to activators and inhibitors has allowed classification of serine/threonine protein phosphatases (PPs) into four major types designated types 1, 2A, 2B and 2C (PP1, PP2A, PP2B and PP2C, respectively). Comparison of sequences within their catalytic domains has indicated that PP1, PP2A and PP2B are members of the same gene family named PPP. On the other hand, the type 2C enzyme does not share sequence homology with the PPP members and thus represents another gene family, known as PPM. In this report we briefly summarize some of our studies about the role of serine/threonine phosphatases in growth and differentiation of three different eukaryotic models: Blastocladiella... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Protein phosphatases; Blastocladiella emersonii; Neurospora crassa; Dictyostelium discoideum. |
| Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000700006 |
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| Ferreira-Nozawa,M.S.; Rezende,J.L.; Guimarães,L.H.S.; Terenzi,H.F.; Jorge,J.A.; Polizeli,M.L.T.M.. |
| Two strains (15.1 and 15.8) of the thermophilic fungus Scytalidium thermophilum produced high levels of intracellular glucoamylases, with potential for industrial applications. The isoform I of the glucoamylase produced by 15.1 strain was sequentially submitted to DEAE-Cellulose and CM-Cellulose chromatography, and purified 141-fold, with 5.45% recovery. The glucoamylase of strain 15.8 was purified 71-fold by CM-Cellulose and Concanavalin A-Sepharose chromatography, with 7.38% recovery. Temperature and pH optima were in the range of 50-60ºC and 5.0-6.0, respectively, using starch and maltose as substrates. The glucoamylase of S. thermophilum 15.8 was more stable (t50 > 60 min) than that of S. thermophilum 15.1 (t50= 11-15 min), at 60ºC. The glucoamylase... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Glucoamylase; Amylase; Scytalidium thermophilum; Thermostable enzyme; Starch hydrolysis. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000200027 |
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