Anacardium occidentale Bark Lectin: Purification, Immobilization as an Affinity Model and Influence in the Uptake of Technetium-99M by Rat Adipocytes

作者：Sucupira Maciel Maria Ines; de Mendonca Cavalcanti Maria do Socorro; Napoleao Thiago Henrique; Guedes Paiva Patricia Maria; Jansem de Almeida Catanho Maria Teresa; Breitenbach Barroso Coelho Luana Cassandra

来源：Applied Biochemistry and Biotechnology, 2012, 168(3): 580-591.

DOI：10.1007/s12010-012-9798-1

• Anacardium occidentale
• Lectin
• Affinity matrix
• Technetium-99M

Lectins, proteins that recognize carbohydrates, have been immobilized on inert supports and used in the screening or purification of glycoproteins. Anacardium occidentale bark infusion has been used as a hypoglycemic agent in Brazil. The toxicity of natural products may be evaluated determining their capability to alter the biodistribution of technetium-99M (Tc-99m). This work reports the isolation and characterization of a lectin from A. occidentale bark (AnocBL), its evaluation as an affinity support for glycoprotein isolation and lectin effect on the uptake of Tc-99m by rat adipocytes. AnocBL was isolated from 80 % ammonium sulphate supernatant by affinity chromatography on fetuin-agarose. SDS-PAGE showed a single protein band of 47 kDa. The monossacharide l-arabinose and the glycoproteins fetuin, asialofetuin, ovomucoid, casein, thyroglobulin, peroxidase, fetal bovine serum and IgG inhibited the activity. The lectin activity was stable until 70 A degrees C and at a pH range of 3.0-7.5. AnocBL-Sepharose column bound fetuin indicating that the lectin matrix may be used to obtain glycoconjugates of biotechnological interest. In vitro assay revealed that glucose and insulin increase Tc-99m uptake by rat adipocytes. AnocBL decreases Tc-99m uptake, and this effect was not detected in the presence of glucose. Fetuin inhibited AnocBL effect in all insulin concentrations.

• 出版日期2012-10