João Batista Cajazeiras

Learn More
Recent studies have shown that lectins are promising tools for use in various biotechnological processes, as well as studies of various pathological mechanisms, isolation, and characterization of glycoconjugates and understanding the mechanisms underlying pathological mechanisms conditions, including the inflammatory response. This study aimed to purify,(More)
Lectins are proteins that have the ability to bind specifically and reversibly to carbohydrates and glycoconjugates, without altering the structure of the glycosyl ligand. They are found in organisms such as viruses, plants and humans, and they have been shown to possess important biological activities. The objective of this study was to purify and(More)
In order to produce transgenic goats with hG-CSF, a total of 24 adult Saanen and 48 adult undefined breed goats were used as donors and recipients, respectively. Donors were estrus-synchronized with vaginal sponges and superovulated by a treatment with 200 mg FSH given twice daily in decreasing doses over 3 days starting 48 h before sponge removal.(More)
Here, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of proteins. ConM was crystallized and its structure determined by standard molecular replacement techniques. The(More)
Lectin from the seeds of Dioclea sclerocarpa (DSL) was purified in a single step by affinity chromatography on a Sephadex G-50 column. The primary sequence, as determined by tandem mass spectrometry, revealed a protein with 237 amino acids and 81% of identity with ConA. DSL has a molecular mass of 25,606 Da. The β and γ chains weigh 12,873 Da and 12,752 Da,(More)
A novel mannose/glucose-binding lectin from Canavalia virosa (designated as ConV) has been purified from seeds of C. virosa by affinity chromatography on a mannose-Sepharose 4B column. ConV strongly agglutinates rabbit erythrocytes and was inhibited by monosaccharides (D-mannose, D-glucose, and α-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin).(More)
Lectins are proteins or glycoproteins with the ability to link to carbohydrates at the cell surface in a specific and reversible manner. Studies have showed that lectins are demonstrate immunomodulatory and antitumor agents. This study aims to evaluate the effect of lectin extracted from the seeds of Canavalia brasiliensis (ConBr) on murine melanoma B16F10(More)
Lectins constitute a class of glycoproteins, which are capable of selectively and reversibly binding to carbohydrates, distinguishing small structural differences in complex oligosaccharides. Studies have shown that the binding of lectins to cell-surface carbohydrates can lead to various effects such as cellular proliferation, histamine release and cytokine(More)
Lectin from the seeds of Dioclea lasiophylla (DlyL) was purified in a single step by affinity chromatography on a Sephadex® G-50 column. DlyL strongly agglutinated rabbit erythrocytes and was inhibited by monosaccharides (D-mannose and α-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin). Similar to other Diocleinae lectins, DlyL has three chains,(More)
A lectin from seeds of Dioclea lasiocarpa (DLL) was purified in a single step by affinity chromatography in a Sephadex G-50 column. DLL haemagglutinated rabbit erythrocytes showing stability even after 1 h of exposure to a different pH values (optimal between pH 6.0 and 8.0) but was inhibited after incubation with D-mannose and D-glucose. The pure protein(More)