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RISS 인기검색어
- 검색키워드
- 저자 : Shunmugiah Karutha Pandian (검색결과 3 건)
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Subramani Pandian,Karuppasamy Marichelvam,Lakkakula Satish,Stanislaus Antony Ceasar,Shunmugiah Karutha Pandian,Manikandan Ramesh 한국작물학회 2018 Journal of crop science and biotechnology Vol.21 No.5
Finger millet is an important staple food crop of semi-arid tropics also known as “super cereal” and has a higher calcium content than any other crops. Thousands of germplasm are being maintained and its genetic characterization is essential for further utilization in crop improvement. This research was performed to estimate the diversity and population genetic structure in the mini-core collection of finger millet by using SPAR markers, namely RAPD, ISSR, and DAMD markers. Altogether, 32 primers were used in this study, which produced 408 bands among which 344 were polymorphic. Analysis by combining all three marker systems revealed 84.31% of polymorphism among 90 genotypes of finger millet. Average polymorphism information content (PIC) produced by the ISSR, RAPD, and DAMD markers were 0.79, 0.81, 0.62, and average Rp values were 12.84, 8.17, and 8.53, respectively. The Jaccard's similarity value ranged from 0.233-0.861. IE 6059 and IE 5870 genotypes showed the highest Jaccard's similarity value of 0.861 in UPGMA analysis. Neighbor joining-based phylogenetic analysis produced two major clusters and the genotypes were grouped based on their geographical region of origin. Principal component analysis and principal coordinates analysis also confirmed the results. In population STRUCTURE analysis, the genotypes were divided into two subpopulations (P1and P2). These results confirmed that the genotypes we have assessed were genetically diverse and were clustered based on their geographic region of origin. The information obtained from this study will be useful in population management strategies and selection of genotypes for an effective breeding program in the future.
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Changes in Caenorhabditis elegans Exposed to Vibrio parahaemolyticus
( Durai Sellegounder ),( Shunmugiah Karutha Pandian ),( Krishnaswamy Balamurugan ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.10
Vibrio parahaemolyticus, which owes its origin to the marine environment, is considered as one of the most common causes of infectious diarrhea worldwide. The present study investigated the pathogenicity of V. parahaemolyticus against the model organism, Caenorhabditis elegans. Infection in the host was localized with GFP-tagged V. parahaemolyticus using confocal laser scanning microscopy. The times required for causing infection, bacterial load in intestine, chemotactic response, and alteration in pharyngeal pumping were analyzed in the host system. In addition, the regulation of innate immune-related genes, lys-7, clec- 60, and clec-87, was analyzed using real-time PCR. The role of immuneresponsible pmk-1 was studied using mutant strains. The pathogenicity of environmental strain CM2 isolated from the Gulf of Mannar, India was compared with that of a reference strain obtained from ATCC. The pathogen infected animals appeared to ward off infection by upregulating candidate antimicrobial genes for a few hours after the exposure, before succumbing to the pathogen. For the first time, the pathogenicity of V. parahaemolyticus at both the physiological and molecular levels has been studied in detail using the model organism C. elegans.
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( Kalibulla Syed Ibrahim ),( Jeyaraj Muniyandi ),( Shunmugiah Karutha Pandian ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.1
The purification and characterization of a Mn2+-dependent alkaline serine protease produced by Bacillus pumilus TMS55 were investigated. The enzyme was purified in three steps: concentrating the crude enzyme using ammonium sulfate precipitation, followed by gel filtration and cation-exchange chromatography. The purified protease had a molecular mass of approximately 35 kDa, was highly active over a broad pH range of 7.0 to 12.0, and remained stable over a pH range of 7.5 to 11.5. The optimum temperature for the enzyme activity was found to be 60oC. PMSF and AEBSF (1 mM) significantly inhibited the protease activity, indicating that the protease is a serine protease. Mn2+ ions enhanced the activity and stability of the enzyme. In addition, the purified protease remained stable with oxidants (H2O2, 2%) and organic solvents (25%), such as benzene, hexane, and toluene. Therefore, these characteristics of the protease and its dehairing ability indicate its potential for a wide range of commercial applications.
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