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Appl Biochem Biotechnol ; 164(6): 741-54, 2011 Jul.
Article in English | MEDLINE | ID: mdl-21340539

ABSTRACT

The lectin from seeds of Dioclea virgata (DvirL) was purified in a single step affinity chromatography, sequenced by tandem mass spectrometry and submitted to crystallization and biological experiments. DvirL has a molecular mass of 25,412 ± 2 Da and the chains ß and γ has 12,817 Da ± 2 and 12,612 Da ± 2, respectively. Primary sequence determination was assigned by tandem mass spectrometry and revealed a protein with 237 amino acids and 87% of identify with ConA. The protein crystals were obtained native and complexed with X-Man using vapor-diffusion method at a constant temperature of 293 K. A complete X-ray dataset was collected at 1.8 Å resolution. DvirL crystals were found to be orthorhombic, belonging to the space group I222, with a unit cell parameters a = 647.5 Å, b = 86.6 Å, c = 90.2 Å. Molecular replacement search found a solution with a correlation coefficient of 77.1% and an R(factor) of 44.6%. The present study also demonstrated that D. virgata lectin presents edematogenic and antinociceptive activities in rodents electing this protein as a candidate to structure/function analysis.


Subject(s)
Analgesics/chemistry , Dioclea/chemistry , Plant Lectins/chemistry , Amino Acid Sequence , Analgesics/isolation & purification , Analgesics/pharmacology , Animals , Crystallization , Edema/drug therapy , Humans , Male , Mass Spectrometry , Mice , Molecular Sequence Data , Peptide Mapping , Plant Lectins/isolation & purification , Plant Lectins/pharmacology , Seeds/chemistry , Sequence Alignment , X-Ray Diffraction
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