4 resultados para 324.1

em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"


Relevância:

60.00% 60.00%

Publicador:

Resumo:

The objective was to evaluate the internal quality of white-shelled consume eggs, sanitized or not, stored under different packaging conditions at room temperature. It was used 300 eggs, distributed in a completely randomized experimental design in a 3×2×4+1 factorial arrangement, three packaging conditions (PVC film, partial vacuum, partial vacuum with oxygen gas absorber), storage period (7, 14, 21 and 28 days), sanitized or not, and control (fresh eggs), with four repetitions. At the end of each period the analysis were performed. Partial vacuum condition was able to maintained Haugh unit, and promoted the best results for yolk index. The weight maintenance was better when packaged under vacuum, with or without O2 sachets absorbers. Lower values of water activity were obtained in eggs packed in PVC film, and when the sanitation was performed. It can be concluded that the internal egg quality decreases with storage time sharper in the eggs packed in PVC film, because vacuum has preserved some features of them. With sanitation, the storage conditions of eggs in PVC film should be improved because its internal quality decrease was greatest.

Relevância:

30.00% 30.00%

Publicador:

Resumo:

Even being a bacterial purine nucleoside phosphorylase (PNP), which normally shows hexameric folding, the Mycobacterium tuberculosis PNP (MtPNP) resembles the mammalian trimeric structure. The crystal structure of the MtPNP apoenzyme was solved at 1.9 Angstrom resolution. The present work describes the first structure of MtPNP in complex with phosphate. In order to develop new insights into the rational drug design, conformational changes were profoundly analyzed and discussed. Comparisons over the binding sites were specially studied to improve the discussion about the selectivity of potential new drugs. (C) 2004 Elsevier B.V. All rights reserved.

Relevância:

30.00% 30.00%

Publicador:

Resumo:

Roscovitine and flavopiridol have been shown to potently inhibit cyclin-dependent kinase 1 and 2 (CDK1 and 2). The structures of CDK2 complexed with roscovitine and deschoroflavopiridol have been reported, however no crystallographic structure is available for complexes of CDK1 with inhibitors. The present work describes two molecular models for the binary complexes CDK1:roscovitine and CDK1:flavopiridol. These structural models indicate that both inhibitors strongly bind to the ATP-binding pocket of CDKI and structural comparison of the CDK complexes correlates the structures with differences in inhibition of these CDKs by flavopiridol and roscovitine. This article explains the structural basis for the observed differences in activity of these inhibitors. (C) 2004 Elsevier B.V. All rights reserved.