The leaves of Chenopodium album Linn. are traditionally used for treatment of kidney diseases and urinary stones. The present work investigated the effect of aqueous extract of leaves of C. album (CAAE) on in-vitro crystallization of CaOx and brushite crystals. Crystallization was studied by using nucleation and aggregation assay of calcium oxalate (CaOx) crystals and growth assay of calcium oxalate monohydrate and brushite crystals. The effects of CAAE and cystone on slope of nucleation and aggregation as well as growth of calcium oxalate crystallization were evaluated spectrophotometrically. The densities of the formed crystals were compared under microscope. The effects of CAAE and citric acid on growth of brushite crystals were studied by using single diffusion gel growth technique, and the parameters evaluated were length, morphology and average size of the deposited crystals. CAAE significantly inhibited the slope of nucleation and aggregation of CaOx crystallization, and decreased the crystal density. It also inhibited the growth and caused the dissolution of brushite crystals. The standard drug cystone or citric acid also exhibited similar effects. The study reveals that the leaves of C. album were found effective in the prevention of the experimentally induced urinary stones and substantiate the traditional claim. It is concluded that the leaves of C. album have beneficial inhibitory effect on in-vitro crystallization of CaOx and CHPD (brushite) crystals.
Botulism is a neuroparalytic disease caused by Clostridium botulinum, which produces seven (A-G) neurotoxins (BoNTs). The mouse bioassay is the gold standard for the detection of botulinum neurotoxins, however it requires at least 3-4 days for completion. Most of the studies were carried out in botulinum toxin A and less on type B. Attempts have been made to develop an ELISA based detection system, which is potentially an easier and more rapid method of botulinum neurotoxin detection. In the present study, the synthetic BoNT/B LC gene was constructed using PCR overlapping primers, cloned in a pET28a+ vector and expressed in E. coli BL21DE3. The maximum yield of recombinant proteins was optimized after 16 hrs of post induction at 21°C and purified the recombinant protein in soluble form. Antibodies were raised in Mice and Rabbit. The IgG antibody titer in the case of Mice was 1: 1,024,000 and Rabbit was 1: 512,000 with alum as adjuvant via intramascular route. The biological activity of the recombinant protein was confirmed by in-vitro studies using PC12 cells by the synaptobrevin cleavage, the rBoNT/B LC protein showed the maximum blockage of acetylcholine release at a concentration of 150nM rBoNT/B LC in comparison to the control cells. When the cells were incubated with rBoNT/B LC neutralized by the antisera raised against it, the acetylcholine release was equivalent to the control. IgG specific to rBoNT/B LC was purified from raised antibodies. The results showed that the developed antibody against rBoNT/B LC protein were able to detect botulinum toxin type B approximately up to 1 ng/ml. These developed high titer antibodies may prove useful for the detection of botulinum neurotoxins in food and clinical samples.
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