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Group III PLA2 from the scorpion, Mesobuthus tamulus: cloning and recombinant expression in E. coli Electron. J. Biotechnol.
Hariprasad,Gururao; Saravanan,Kolandaivelu; Singh,Sundararajan Baskar; Das,Utpal; Sharma,Sujata; Kaur,Punit; Singh,Tej Pal; Srinivasan,Alagiri.
Phospholipases A2 (PLA2) are enzymes that specifically hydrolyze the sn-2 fatty acid acyl bond of phospholipids, producing a free fatty acid and a lyso-phospholipid. We report the cloning and expression of a secretory phospholipase A2 (sPLA2) from Mesobuthus tamulus, Indian red scorpion. The nucleotide sequence codes for a 167 residue enzyme. The open reading frame codes for a 31 amino acid signal peptide followed by a mature portion of the protein. The primary structure shows the calcium binding motif, catalytic residues, 8 highly-conserved cysteines and C-terminal extension which classify it as a group III PLA2. The entire transcript was expressed in Escherichia coli and was purified by metal affinity chromatography under denaturing conditions. The...
Tipo: Journal article Palavras-chave: Group III phospholipase A2; Mesobuthus tamulus; Recombinant expression.
Ano: 2009 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582009000300006
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Molecular characteristics, recombinant expression and activity detection of OsGSTL1 from rice BABT
Hu,Tingzhang; Yang,Yongwei; Tan,Lili; Yang,Junnian; Wu,Yingmei.
The mRNA of OsGSTL1 was detected in the roots and leaves of rice plants at seedling and tillering stages, and their roots, leaves and panicles at the heading stage. The full-length open reading frame of OsGSTL1 cDNA was 732 bp and encoded a putative polypeptide of 243 amino acids with a calculated molecular mass of 27.30 kDa and a theoretical pI of 5.50. The protein sequences of OsGSTL1 exhibited typical feature of the lambda class GST, which contained the conserved domain "GST_C_Lambda" in C-terminal alpha helical domain and a highly conserved Cys42 in active center. In silico predictions showed that the OsGSTL1 protein was strongly hydrophilic. The phylogenetic analysis revealed OsGSTL1 belonged to monocots subgroup and was closer to IN2-1 of Z. may. The...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glutathione S-transferase; GST activity; In silico; Oryza sativa L.; Recombinant expression; Semi-quantitative RT-PCR.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000100011
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Recombinant expression and refolding of the c-type lysozyme from Spodoptera litura in E. coli Electron. J. Biotechnol.
Kim,Jong-Wan; Yoe,Jeehyun; Lee,Gil Ho; Yoe,Sung Moon.
The chicken-type lysozyme of the insect Spodoptera litura (SLLyz) is a polypeptide of 121 amino acids containing four disulfide bridges and 17 rare codons and participates in innate defense as an anti-bacterial enzyme. The recombinant S. litura lysozyme (rSLLyz) expressed as a C-terminal fusion protein with glutathione S-transferase (GST) in Rosetta(DE3) Singles. The protein was produced as an inclusion body which was solubilized in 8 M urea, renatured by on-column refolding, and purified by reversed-phase chromatography to 95% purity. The purified rSLLyz demonstrated antibacterial activity against B. megaterium confirmed by inhibition zone assay. The overexpression and refolding strategy described in this study will provide a reliable technique for...
Tipo: Journal article Palavras-chave: Antibacterial activity; Inclusion body; Lysozyme; On-column refolding; Recombinant expression; Spodoptera litura.
Ano: 2011 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000300006
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