| dc.date | 2015 | |
| dc.date | 2016-06-03T20:13:11Z | |
| dc.date | 2016-06-03T20:13:11Z | |
| dc.date.accessioned | 2018-03-29T01:32:20Z | |
| dc.date.available | 2018-03-29T01:32:20Z | |
| dc.identifier | | |
| dc.identifier | Journal Of Biomolecular Techniques. Association Of Biomolecular Resource Facilities, v. 26, n. 3, p. 90 - 102, 2015. | |
| dc.identifier | 15240215 | |
| dc.identifier | 10.7171/jbt.15-2603-002 | |
| dc.identifier | http://www.scopus.com/inward/record.url?eid=2-s2.0-84940201611&partnerID=40&md5=c1800a143391427693d64c9fd8dcf5e1 | |
| dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/237993 | |
| dc.identifier | 2-s2.0-84940201611 | |
| dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1304654 | |
| dc.description | In this study, the aim was to determine the complete sequence of the Copaifera langsdorffii trypsin inhibitor (CTI)- 1 using 2-dimensional (2D)-PAGE, matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF), and quadrupole time-of-flight (QTOF) spectrometry. Spots A (CTI-1) and F (CTI-2) were submitted to enzymatic digestions with trypsin, SV8, and clostripain. The accurate mass of the peptide obtained from each digest was determined by mass spectrometry (MS) using MALDI-TOF. The most abundant peptides were purified and sequenced in a liquid chromatograph connected to an electrospray ionization-QTOF MS. When the purified trypsin inhibitor was submitted to 2D electrophoresis, different spots were observed, suggesting that the protein is composed of 2 subunits with microheterogeneity. Isoelectric points of 8.0, 8.5, and 9.0 were determined for the 11 kDa subunit and of 4.7, 4.6, and 4.3 for the 9 kDa subunit. The primary structure of CTI-1, determined from the mass of the peptide of the enzymatic digestions and the sequence obtained by MS, indicated 180 shared amino acid residues and a high degree of similarity with other Kunitz (KTI)-type inhibitors. The peptide also contained an Arg residue at the reactive site position. Its 3-dimensional structure revealed that this is because the structural discrepancies do not affect the canonical conformation of the reactive loop of the peptide. Results demonstrate that a detailed investigation of the structural particularities of CTI-1 could provide a better understanding of the mechanism of action of these proteins, as well as clarify its biologic function in the seeds. CTI-1 belongs to the KTI family and is composed of 2 polypeptide chains and only 1 disulfide bridge. © 2015 ABRF. | |
| dc.description | 26 | |
| dc.description | 3 | |
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| dc.description | | |
| dc.language | en | |
| dc.publisher | Association of Biomolecular Resource Facilities | |
| dc.relation | Journal of Biomolecular Techniques | |
| dc.rights | fechado | |
| dc.source | Scopus | |
| dc.title | Primary Structure Of A Trypsin Inhibitor (copaifera Langsdorffii Trypsin Inhibitor-1) Obtained From C. Langsdorffii Seeds | |
| dc.type | Artículos de revistas | |
