18 resultados para Food - Labeling


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It is well known that wrist pulse signals contain information about the status of health of a person and hence diagnosis based on pulse signals has assumed great importance since long time. In this paper the efficacy of signal processing techniques in extracting useful information from wrist pulse signals has been demonstrated by using signals recorded under two different experimental conditions viz. before lunch condition and after lunch condition. We have used Pearson's product-moment correlation coefficient, which is an effective measure of phase synchronization, in making a statistical analysis of wrist pulse signals. Contour plots and box plots are used to illustrate various differences. Two-sample t-tests show that the correlations show statistically significant differences between the groups. Results show that the correlation coefficient is effective in distinguishing the changes taking place after having lunch. This paper demonstrates the ability of the wrist pulse signals in detecting changes occurring under two different conditions. The study assumes importance in view of limited literature available on the analysis of wrist pulse signals in the case of food intake and also in view of its potential health care applications.

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The current study analysed how the climbing perch Anabas testudineus an air-breathing freshwater fish make choice when a pair of food patches differing in the gain is presented. The results revealed no significant variation in the preference towards the patch of food material cumulated in one place over the same amount of food dispersed in a wider area and located at an equal distance. Additionally, enhancement of the value of dispersed or cumulated patch, by moving it towards the subject fish (spatial discounting) was also found to be ineffective in influencing the food patch utilisation in this species.

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(p) ppGpp, a secondary messenger, is induced under stress and shows pleiotropic response. It binds to RNA polymerase and regulates transcription in Escherichia coli. More than 25 years have passed since the first discovery was made on the direct interaction of ppGpp with E. coli RNA polymerase. Several lines of evidence suggest different modes of ppGpp binding to the enzyme. Earlier cross-linking experiments suggested that the beta-subunit of RNA polymerase is the preferred site for ppGpp, whereas recent crystallographic studies pinpoint the interface of beta'/omega-subunits as the site of action. With an aim to validate the binding domain and to follow whether tetra-and pentaphosphate guanosines have different location on RNA polymerase, this work was initiated. RNA polymerase was photo-labeled with 8-azido-ppGpp/8-azido-pppGpp, and the product was digested with trypsin and subjected to mass spectrometry analysis. We observed three new peptides in the trypsin digest of the RNA polymerase labeled with 8-azido-ppGpp, of which two peptides correspond to the same pocket on beta'-subunit as predicted by X-ray structural analysis, whereas the third peptide was mapped on the beta-subunit. In the case of 8-azido-pppGpp-labeled RNA polymerase, we have found only one cross-linked peptide from the beta'-subunit. However, we were unable to identify any binding site of pppGpp on the beta-subunit. Interestingly, we observed that pppGpp at high concentration competes out ppGpp bound to RNA polymerase more efficiently, whereas ppGpp cannot titrate out pppGpp. The competition between tetraphosphate guanosine and pentaphosphate guanosine for E. coli RNA polymerase was followed by gel-based assay as well as by a new method known as DRaCALA assay.