|
|
|
|
|
| Di Ciero,Luciana; Bellato,Cláudia de M.; Meinhardt,Lyndel W.; Ferrari,Fernanda; Castellari,Rafael R.; Marangoni,Sérgio; Novello,José C.. |
| Four different detergents, ASB 14, SB 3-10, CHAPS and Triton X100, were utilized to determine the optimal detergent for the solubilization of membrane proteins from the phytopathogenic bacterium Xylella fastidiosa. These proteins were differentially solubilized in distinct buffers containing the detergent and subjected to bidimensional electrophoresis within the non-linear pH range of 3-10. The detergents ASB 14 and SB 3-10 were the most effective revealing 221 and 157 spots, respectively. CHAPS and Triton X100 were less effective and revealed only 72 and 43 spots, respectively. MALDI-TOF tryptic peptide mass fingerprinting of 18 excised proteins from the ASB 14 treatment revealed that 83% were membrane proteins and that the theoretical efficiency of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: X. fastidiosa; 2-DE; Extraction; Proteome; Solubilization. |
| Ano: 2004 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000200018 |
| |
|
|
| Silva,José Antonio da; Pompeu,Dávia Guimarães; Costa,Olavo Flores da; Gonçalves,Daniel Bonoto; Spehar,Carlos Roberto; Marangoni,Sérgio; Granjeiro,Paulo Afonso. |
| Chenopodium quinoa seeds have high protein content. The nutritional value of quinoa is superior compared with traditional cereals. Its essential amino acid composition is considered next to the ideal, and its quality matches that of milk proteins. In this study, the seed storage proteins from Chenopodium quinoa were extracted, fractionated, partially purified, and characterized. The structural characterization was performed by Tricine-SDS-PAGE and two-dimensional electrophoresis, and it confirmed the presence of proteins of molecular weight of 30 and 7kDa, probably corresponding to lectins and trypsin inhibitors, respectively. The functional characterization of these proteins evidenced their activity as antinutritional factors due to their in vitro... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Chenopodium quinoa; Seeds; Lectins; Protease inhibitor; In vitro digestibility. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000100074 |
| |
|
|
| Pesoti,Aline Regiele; Oliveira,Bruno Menezes de; Oliveira,Augusto Cesar de; Pompeu,Dávia Guimarães; Gonçalves,Daniel Bonoto; Marangoni,Sérgio; Silva,José Antonio da; Granjeiro,Paulo Afonso. |
| Abstract A novel trypsin inhibitor of protease (CqTI) was purified from Chenopodium quinoa seeds. The optimal extracting solvent was 0.1M NaCl pH 6.8 (p < 0.05). The extraction time of 5h and 90 °C was optimum for the recovery of the trypsin inhibitor from C. quinoa seeds. The purification occurred in gel-filtration and reverse phase chromatography. CqTI presented active against commercial bovine trypsin and chymotrypsin and had a specific activity of 5,033.00 (TIU/mg), which was purified to 333.5-fold. The extent of purification was determined by SDS-PAGE. CqTI had an apparent molecular weight of approximately 12KDa and two bands in reduced conditions as determined by Tricine-SDS-PAGE. MALDI-TOF showed two peaks in 4,246.5 and 7,908.18m/z. CqTI... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Purification; Characterization; Inhibitor of trypsin; Chenopodium quinoa; Seeds. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400588 |
| |
|
| |
|
|
|
