• Title/Summary/Keyword: Molecular characterization

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Molecular Characterization of Gastrothylax crumenifer (Platyhelminthes: Gastrothylacidae) from Goats in the Western Part of India by LSU of Nuclear Ribosomal DNA

  • Kumar, Ashwani;Chaudhary, Anshu;Verma, Chandni;Singh, Hridaya Shanker
    • Parasites, Hosts and Diseases
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    • 제52권6호
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    • pp.701-705
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    • 2014

  • The rumen parasite, Gastrothylax crumenifer (Platyhelminthes: Gastrothylacidae), is a highly pathogenic trematode parasite of goat (Capra hircus). It sucks blood that causes acute disease like anemia, and severe economic losses occur due to morbidity and mortality of the ruminant infected by these worms. The study of these rumen paramphistomes, their infection, and public health importance remains unclear in India especially in the western part of state Uttar Pradesh (U.P.), Meerut, India, where the goat meat consumption is very high. This paper provides the molecular characterization of G. crumenifer recovered from the rumen of Capra hircus from Meerut, U.P., India by the partial sequence of 28S rDNA. Nucleotide sequence similarity searching on BLAST of 28S rDNA from parasites showed the highest identity with those of G. crumenifer from the same host Capra hircus. This is the first report of molecular identification of G. crumenifer from this part of India.

  • https://doi.org/10.3347/kjp.2014.52.6.701 인용 PDF KSCI

Purification and characterization of a thermostable glutamate dehydrogenase from a thermophilic bacterium isolated from a sterilization drying oven

  • Amenabar, Maximiliano J.;Blamey, Jenny M.
    • BMB Reports
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    • 제45권2호
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    • pp.91-95
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    • 2012

  • Glutamate dehydrogenase from axenic bacterial cultures of a new microorganism, called GWE1, isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular-exclusion liquid chromatography. The apparent molecular mass of the native enzyme was 250.5 kDa and was shown to be an hexamer with similar subunits of molecular mass 40.5 kDa. For glutamate oxidation, the enzyme showed an optimal pH and temperature of 8.0 and $70^{\circ}C$, respectively. In contrast to other glutamate dehydrogenases isolated from bacteria, the enzyme isolated in this study can use both $NAD^+$ and $NADP^+$ as electron acceptors, displaying more affinity for $NADP^+$ than for $NAD^+$. No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. The enzyme was exceptionally thermostable, maintaining more than 70% of activity after incubating at $100^{\circ}C$ for more than five hours suggesting being one of the most thermoestable enzymes reported in the family of dehydrogenases.

  • https://doi.org/10.5483/BMBRep.2012.45.2.91 인용 PDF KSCI