Corporate valuation: theoretical postulates and empirical evidence from SENSEX firms in India

Corporate valuation forms as one of the most significant pillars in the field of finance. With refinements in academic theories surrounding asset-pricing models and advancements in computing technology, studies in this field have generated an enormous amount of interest among academics and practitioners alike. In this paper, the author seeks to investigate the above research phenomenon by resorting to an empirical examination carried out on a sample comprising of the firms forming part of India’s benchmark market index – SENSEX. As a prelude to the scientific procedure outlining the above, the author discusses all the significant theoretical postulates surrounding the corporate valuation led by the Discounted Cash Flow (DCF) analysis. Upon the empirical investigation surrounding the corroboration of intrinsic measure of corporate values with the market-determined counterparts, the author finds statistically significant evidence refuting the null hypothesis underlying the indifference between intrinsically-determined enterprise values and market-determined enterprise values. Such an observation throws up interesting research possibilities. One, the author might wish to decipher arguments against the phenomenon underlying ‘market efficiency’, as the same would obliterate any attempt made by a discerning investor to earn ‘abnormal return’ on her investment. Second, the author might wish to substantiate the arguments forwarded by the iconic breed of investors subscribing to the ‘value investing’ philosophy by reasoning out the need to identify prospective investment opportunities available against a vast expanse of securities founded on a calibrated notion of ‘fundamental approach towards investments

Ecological status of the lion-tailed Macaque and its rainforest habitats in Karnataka, India

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Kudremukh Iron Ore Company Limited (KIOCL): the death Knell and beyond

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Carnivore conservation at the crossroads

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Functional analysis of various conserved domains of NPH3 involved in phototropism in Arabidopsis thaliana

Abstract only availablePhototropism - the directional growth (curvature) for a plant towards light, is a very important adaptive response in plants in order for them to maximize photosynthesis. Blue light triggers phototropic response in Arabidopsis thaliana via the dominant photoreceptor phototropin 1 (phot1). Genetic studies have identified several genes that encode phot1 interacting proteins. Of these, currently, only NON PHOTOTROPIC HYPOCOTYL 3 (NPH3) is known to be absolutely required for phototropism. nph3 mutants are completely aphototropic, resembling phot1 null mutants. NPH3 is a phosphoprotein containing a BTB and a coiled coil domain, and the dephosphorylation of this protein into its active state in light is known to be entirely phot1 dependant. Yet little is known of the role of NPH3 as a mediator in the phototropic signal-response pathway. To better understand the role of conserved domains of NPH3 in phototropism, a range of serial deletions and mutants of NPH3 were generated, driven by its own native NPH3 promoter and the constitutive CaMV 35S promoter in nph3-6 and wild-type Col-0 backgrounds respectively. All truncated and mutant NPH3 proteins were also translationally fused with a green fluorescent protein (GFP). Multiple T3 homozygous transgenic lines were evaluated by comparing average angles of hypocotyl curvature with those of aphotoropic nph3-6 and wild-type Col-0. Over-expression of NPH3 or different portions of NPH3 in Col-0 resulted in reduced phototropism. Selective expression of the NPH3 domains under the native promoter could not complement the null nph3-6 phenotype. The alterations in the subcellular localization of these transgenic lines were also investigated using confocal fluorescence microscopy.NSF Plant Genomics Internship @ M

Phosphorylation of rat spermatidal protein TP2 by sperm-specific protein kinase A and modulation of its transport into the haploid nucleus

Transition protein 2 (TP2), which is expressed during stages 12-15 of mammalian spermiogenesis, has been shown to undergo phosphorylation immediately after its synthesis. We reported earlier that TP2 is phosphorylated in vitro at threonine 101 and serine 109 by the salt extract of sonication-resistant (elongating and elongated) spermatid nuclei and the protein kinase phosphorylating TP2 was identified to be protein kinase A (PKA). We now report that the cytosol from haploid spermatids but not from premeiotic germ cells is able to phosphorylate recombinant TP2 in vitro at threonine 101 and serine 109. The kinase present in the haploid spermatid cytosol that phosphorylates TP2 has been identified to be the sperm-specific isoform of protein kinase A (Cs-PKA). Reverse transcription-PCR analysis indicated that Cs-PKA was present in the haploid spermatids and absent from premeiotic germ cells. The rat Cs-PKA transcript was amplified and sequenced using the isoform-specific primers. The sequence of rat Cs-PKA at the N terminus differs from mouse and human by one amino acid. Western blot analysis using specific anti-Cα1 antibodies revealed that Cα1-PKA is absent in haploid spermatid cytosol. We have also established an in vitro nuclear transport assay for the haploid round spermatids. Using this assay, we have found that the cytoplasmic factors and ATP are absolutely essential for translocation of TP2 into the nucleus. Phosphorylation was found to positively modulate the NLS dependent import of TP2 into the nucleus