Shape from Sound: Toward New Tools for Quantum Gravity

To unify general relativity and quantum theory is hard in part because they are formulated in two very different mathematical languages, differential geometry and functional analysis. A natural candidate for bridging this language gap, at least in the case of the Euclidean signature, is the discipline of spectral geometry. It aims at describing curved manifolds in terms of the spectra of their canonical differential operators. As an immediate benefit, this would offer a clean gauge-independent identification of the metric’s degrees of freedom in terms of invariants that should be ready to quantize. However, spectral geometry is itself hard and has been plagued by ambiguities. Here, we regularize and break up spectral geometry into small, finite-dimensional and therefore manageable steps. We constructively demonstrate that this strategy works at least in two dimensions. We can now calculate the shapes of two-dimensional objects from their vibrational spectra

Statistically Designed Bioprocess for Enhanced Production of Alkaline Protease in Bacillus cereus HP_RZ17

491-498Alkaline protease is one of the bulk enzymes having wide commercial demand for various applications. It is commercially produced by a submerged fermentation process employing various bacteria, Bacillus sp. being the most widely used species. Statistical optimization of the process for the production of alkaline proteases from rhizospheric bacteria and its application in the biocontrol of plant pathogens has not been explored fully and needs to be studied for the development of efficient bioprocess. We report the enhanced production of alkaline protease in the minimal salt medium (MSM) optimized using statistical approaches such as Plackett Burman Design (PBD) and Response Surface Methodology (RSM). In the first step; PBD, among the total eight variables, three variables namely, yeast extract (pppBacillus cereus HP_RZ17. These three variables were further analyzed in the second step i.e. Central Composite Design (CCD) of RSM. The optimum yield of alkaline protease by B. cereus HP_RZ17 (130.72 UmL-1) was obtained under the optimal conditions such as yeast extract (0.899% w/v), fructose (0.873% w/v), and pH (11.25) of production media. The statistically optimized values of variables used for the scale-up of the process at 5 L capacity bioreactor enhanced the alkaline protease yield (132.48 UmL-1) by 1.09 fold vis-à-vis un-optimized protocol (121.96 UmL-1) in B. cereus HP_RZ17

Sulforaphane Causes Epigenetic Repression of hTERT Expression in Human Breast Cancer Cell Lines

Sulforaphane (SFN), an isothiocyanate found in cruciferous vegetables, is a common dietary component that has histone deacetylase inhibition activity and exciting potential in cancer prevention. The mechanisms by which SFN imparts its chemopreventive properties are of considerable interest and little is known of its preventive potential for breast cancer. expression facilitated the induction of cellular apoptosis in human breast cancer cells.Collectively, our results provide novel insights into SFN-mediated epigenetic down-regulation of telomerase in breast cancer prevention and may open new avenues for approaches to SFN-mediated cancer prevention

Statistically designed bioprocess for enhanced production of alkaline protease in bacillus cereus HP_RZ17

Alkaline protease is one of the bulk enzymes having wide commercial demand for various applications. It is commercially produced by a submerged fermentation process employing various bacteria, Bacillus sp. being the most widely used species. Statistical optimization of the process for the production of alkaline proteases from rhizospheric bacteria and its application in the biocontrol of plant pathogens has not been explored fully and needs to be studied for the development of efficient bioprocess. We report the enhanced production of alkaline protease in the minimal salt medium (MSM) optimized using statistical approaches such as Plackett Burman Design (PBD) and Response Surface Methodology (RSM). In the first step; PBD, among the total eight variables, three variables namely, yeast extract (p<0.05), fructose (p<0.05) and pH (p<0.05) influenced the production of alkaline protease by Bacillus cereus HP_RZ17. These three variables were further analyzed in the second step i.e. Central Composite Design (CCD) of RSM. The optimum yield of alkaline protease by B. cereus HP_RZ17 (130.72 UmL-1) was obtained under the optimal conditions such as yeast extract (0.899% w/v), fructose (0.873% w/v), and pH (11.25) of production media. The statistically optimized values of variables used for the scale-up of the process at 5 L capacity bioreactor enhanced the alkaline protease yield (132.48 UmL-1) by 1.09 fold visà-vis un-optimized protocol (121.96 UmL-1) in B. cereus HP_RZ17

Purification of multiple forms of cytochrome P450 from a human brain and reconstitution of catalytic activities

The present study demonstrates the presence of multiple forms of cytochrome P450 (P450) in human brain obtained at autopsy, the purification of various isoforms to apparent homogeneity, and the monooxygenase activities in reconstituted systems. Sequential chromatography on octylamino-Sepharose 4B, DEAE-Sephacel, and DEAE-cellulose yielded four isoforms of P450 (A, B, C, and D) with specific contents of 11.0, 9.4, 12.5, and 8.3 nmol of P450/mg protein, respectively. While the forms A, B, and C were apparently homogeneous as examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; the P450D was not homogeneous. The apparent molecular masses of the four forms of P450 were 60,200 Da (P450A), 60,900 Da (P450B), 60,200 Da (P450C), and 61,000 Da (P450D), respectively. NADPH cytochrome P450 reductase (reductase) was also partially purified from the brain microsomes. Immunoblot analysis of the four forms of human purified P450, using antisera to purified rat liver P450 (IIBL + 11B2), rat liver P450 (1A1 + 1A2), phenobarbital-inducible rat brain P450, human liver P450 IIE 1, P450 1A2, P450 IIC, and P450 IIIA4, indicated differential immunological cross-reactivity. The monooxygenase activities of the purified human brain P450s were demonstrated with various substrates (aminopyrine, morphine, aniline, 7-ethoxycoumaria, and nifedipine) as examined in reconstituted systems consisting of purified human brain P450, purified rat brain NADPH cytochrome P450 reductase, deoxycholate, phospholipid, and NADPH