Assessment of heavy metal in the water,sediment, and two edible fish species of Jamshedpur Urban Agglomeration,India with special emphasis on human health risk

The city of Jamshedpur, nicknamed the “industrial capital of Jharkhand,” is one of the oldest industrial settlements in India, nestled amidst the mineral-rich Chota Nagpur plateau, with its diverse tribal population. Heavy metal contamination from industrialization and urbanization can pose a serious health risk to the resident population of the city. Metal concentrations in water and sediment of various water bodies (rivers, canals, and lakes) were determined using ICP-MS. Pollution indices indicate heavy metal contamination at Jamshedpur Urban Agglomeration, mainly because of Cr (23–1111.6 mg/kg), Hg (0.08–4.11 mg/kg), and Pb (5.2–248 mg/kg). Labeo rohita and Punitus sarara, the two popular edible fishes, also have high concentration of Cr, Hg, and Pb. Health risk to human population due to consumption of metal contaminated edible fishes (L. rohita and P. sarara) was determined by target hazard quotient (THQ) and hazard index (HI). THQ value of fish consumption (most popular protein supplement in the area) was found higher for Cr and Pb when compared with previous literature on fish consumption. Also, HI value ranged from 1.4 to 3.9, suggesting that the children have higher health risks than adults, due to consumption of metal contaminated fishes (especially L. rohita).     

Comparative morphology and ecology of two species of Litomosoides (Nematoda: Filarioidea) of rodents in Florida, with a key to the species of Litomosoides Chandler, 1931

From April 1970 to August 1971, 235 cotton rats (Sigmodon hispidus) and 281 rice rats (Oryzomys palustris) were trapped in salt and fresh water marshes in north-central Florida and examined for natural infections of filarial worms, Litomosoides spp. Cotton rats from both types of marshes were infected (28–44 per cent prevalence), whereas only rice rats from the salt marsh were infected (56 per cent prevalence). Older animals were more commonly infected than younger ones. In cotton rats the worms were located in the pleural cavity, whereas in rice rats the worms were located primarily in the abdominal cavity. Filarial worms from rice rats were transmitted experimentally to laboratory-reared rice rats and cotton rats, but worms from cotton rats were transmitted only to cotton rats. Morphological studies on adult forms and microfilariae indicated that the worms in rice rats were distinct from those in cotton rats and are therefore described as Litomosoides scotti sp. n. The cotton rat filariids were referable to Litomosoides carinii (Travassos, 1919) Vaz, 1934. L. scotti differs from L. carinii in the ratio of the spicules, in the shape of the distal end of the right spicule and in having shorter microfilariae.     

A combination of cation exchange and ligand-affinity chromatography for purification of two molecular species of the folate binding protein in human milk,one equipped with a hydrophobic glycosyl phosphatidylinositol tail: characterization of hydrophobicity and electrical charge

Cation exchange chromatography combined with ligand (methotrexate) affinity chromatography on a column desorbed with a pH-gradient was used for separation and large scale purification of two folate binding proteins in human milk. One of the proteins, which had a molecular size of 27 kDa on gel filtration and eluted from the affinity column at pH 5-6 was a cleavage product of a 100 kDa protein eluted at pH 3-4 as evidenced by identical N-terminal amino acid sequences and a reduction in the molecular size of the latter protein to 27 kDa after cleavage of its hydrophobic glycosylphosphatidyl-inositol tail that inserts into Triton X-100 micelles. Chromatofocusing showed that both proteins possessed multiple isoelectric points within the pH range 7-9. The 100 kDa protein exhibited a high affinity to hydrophobic interaction chromatographic gels, whereas this was only the case with unliganded forms of the 27 kDa protein indicative of a decrease in the hydrophobicity of the protein after ligand binding.