Erythropoietic and bone marrow stimulating activity of terminalia catappa extract: Possible role of nitric oxide signaling.

Aims: We assessed the capacity and mechanism of Terminalia catappa (TC) to induce erythropoiesis in vivo in phenylhydrazine- induced anemic mice. Place and Duration of Study: Sample: This study was carried out at Department of Biochemistry and Center for Biotechnology Research and Training Ahmadu Bello University Zaria, and National Research Institute for Chemical Technology, Zaria. The duration spanned between Jan 2011 and Feb 2012. Methodology: Solvent fractions of Terminalia catappa aqueous extract was used to treat phynylhydrazine-induced anemic mice. Treatment was done for four days, erythropoietic activity of each fraction was assayed by determining the effect of these fractions on intracellular hemoglobin and reticulocyte level from the blood, arginase was also assayed. Bone marrow carbonic anhydrase was assayed to monitor bone marrow erythropoietic stimulation. Results: Terminalia catappa was able to up-regulate the synthesis of intracellular hemoglobin (0.135 ±0.004 μmol/0.1ml) significantly comparable to hydroxyurea (HU) (0.158±0.006 μmol/0.1ml), and normalize the peripheral blood reticulocyte index significantly at P<.05 0.94±0.25% close to the non anemic mice 0.97±0.25% and bone marrow carbonic anhydrase activity. TC inhibited arginase activity significantly (P<.05) comparable to hydroxyurea. Conclusion: The results demonstrate Terminalia catappa extract as an erythropoietic agent that supports normal erythroid differentiation in vivo in phenylhydrazine- induced anemic mice in a synergistic fashion.

Comparison of refolding patterns of erabutoxin b and cardiotoxin 3.10.2 from snake venom.

The refolding patterns of erabutoxin b (a neurotoxin) and cardiotoxin 3.10.2 (from Naja naja siamensis venom) have been studied by reducing both the proteins by treatment with reduced dithiothreitol followed by renaturation by treatment with oxidised dithiothreitol. Isoelectric focusing of the samples trapped at varying time intervals during renaturation of the proteins reveals formation of intermediates in the folding pathway with cardiotoxin 3.10.2. having fewer intermediates than erabutoxin b and faster rate of refolding (1 hr and 3 hr respectively).