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| Baptista,M.S.; Alves,M.J.M.; Arantes,G.M.; Armelin,H.A.; Augusto,O.; Baldini,R.L.; Basseres,D.S.; Bechara,E.J.H.; Bruni-Cardoso,A.; Chaimovich,H.; Colepicolo Neto,P.; Colli,W.; Cuccovia,I.M.; Da-Silva,A.M.; Di Mascio,P.; Farah,S.C.; Ferreira,C.; Forti,F.L.; Giordano,R.J.; Gomes,S.L.; Gueiros Filho,F.J.; Hoch,N.C.; Hotta,C.T.; Labriola,L.; Lameu,C.; Machini,M.T.; Malnic,B.; Marana,S.R.; Medeiros,M.H.G.; Meotti,F.C.; Miyamoto,S.; Oliveira,C.C.; Souza-Pinto,N.C.; Reis,E.M.; Ronsein,G.E.; Salinas,R.K.; Schechtman,D.; Schreier,S.; Setubal,J.C.; Sogayar,M.C.; Souza,G.M.; Terra,W.R.; Truzzi,D.R.; Ulrich,H.; Verjovski-Almeida,S.; Winck,F.V.; Zingales,B.; Kowaltowski,A.J.. |
| The scientific publication landscape is changing quickly, with an enormous increase in options and models. Articles can be published in a complex variety of journals that differ in their presentation format (online-only or in-print), editorial organizations that maintain them (commercial and/or society-based), editorial handling (academic or professional editors), editorial board composition (academic or professional), payment options to cover editorial costs (open access or pay-to-read), indexation, visibility, branding, and other aspects. Additionally, online submissions of non-revised versions of manuscripts prior to seeking publication in a peer-reviewed journal (a practice known as pre-printing) are a growing trend in biological sciences. In this... |
| Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Scientific journals; Scientific editing; Pre-prints; Open access; Peer review. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2019000900401 |
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| Cançado,F.C.; Chimoy Effio,P; Terra,W.R.; Marana,S.R.. |
| cDNA coding for two digestive lysozymes (MdL1 and MdL2) of the Musca domestica housefly was cloned and sequenced. MdL2 is a novel minor lysozyme, whereas MdL1 is the major lysozyme thus far purified from M. domestica midgut. MdL1 and MdL2 were expressed as recombinant proteins in Pichia pastoris, purified and characterized. The lytic activities of MdL1 and MdL2 upon Micrococcus lysodeikticus have an acidic pH optimum (4.8) at low ionic strength (μ = 0.02), which shifts towards an even more acidic value, pH 3.8, at a high ionic strength (μ = 0.2). However, the pH optimum of their activities upon 4-methylumbelliferyl N-acetylchitotrioside (4.9) is not affected by ionic strength. These results suggest that the acidic pH optimum is an intrinsic property of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Lysozyme; Digestive lysozyme; Substrate affinity; PH optimum. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008001100005 |
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