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1.
Food Chem ; 328: 127134, 2020 Oct 30.
Article in English | MEDLINE | ID: mdl-32473493

ABSTRACT

An efficient single quadrupole gas chromatography with mass spectrometry method was developed and validated for the determination of indoxacarb residues in tomato and soil. Residues were extracted from the samples using acetonitrile as extracting solvent and the extracts were purified through primary secondary amine and graphitized carbon black. Recoveries were obtained in the range of 92.12-110.51% with the relative standard deviation of 1.32-4.32%. Indoxacarb dissipated with half-life of 3.12-3.21 and 1.24-1.35d for tomato and soil, respectively following doses of indoxacarb 14.5% SC at 60, 90 and 120 g.a.i./ha. Safe waiting periods were found to be 1-3d. The residues were removed from tomato fruit was in the range of 16.73 to 54.32% using simple decontamination approaches. The present study suggest that the use of indoxacarb in tomato at recommended dose, does not seem to pose any dietary risk to the consumers. The soil RQ values indicated low level of risk to earthworms and arthropods.


Subject(s)
Food Contamination/analysis , Oxazines/analysis , Pesticide Residues/analysis , Soil Pollutants/analysis , Solanum lycopersicum/chemistry , Acetonitriles/chemistry , Dietary Exposure , Food Analysis/methods , Gas Chromatography-Mass Spectrometry , Half-Life , Humans , India , Oxazines/metabolism , Risk Assessment , Soil Pollutants/metabolism , Solvents/chemistry , Time Factors
2.
ISA Trans ; 51(1): 22-9, 2012 Jan.
Article in English | MEDLINE | ID: mdl-21862006

ABSTRACT

The temperature control of a polymerization reactor described by Chylla and Haase, a control engineering benchmark problem, is used to illustrate the potential of adaptive control design by employing a self-tuning regulator concept. In the benchmark scenario, the operation of the reactor must be guaranteed under various disturbing influences, e.g., changing ambient temperatures or impurity of the monomer. The conventional cascade control provides a robust operation, but often lacks in control performance concerning the required strict temperature tolerances. The self-tuning control concept presented in this contribution solves the problem. This design calculates a trajectory for the cooling jacket temperature in order to follow a predefined trajectory of the reactor temperature. The reaction heat and the heat transfer coefficient in the energy balance are estimated online by using an unscented Kalman filter (UKF). Two simple physically motivated relations are employed, which allow the non-delayed estimation of both quantities. Simulation results under model uncertainties show the effectiveness of the self-tuning control concept.


Subject(s)
Chemical Industry/instrumentation , Polymerization , Temperature , Algorithms , Cold Temperature , Computer Simulation , Online Systems , Thermodynamics
3.
Genesis ; 45(9): 570-6, 2007 Sep.
Article in English | MEDLINE | ID: mdl-17868118

ABSTRACT

Temporal colinearity in mouse HoxD is dependent on repressive activity of sequences within the 5' end of the complex. We show that a 5-kb DNA fragment from this region represses transgenes when combined in mouse as well as in Drosophila melanogaster. Moreover, repressive activity in Drosophila depends on some members of the Polycomb-group (PcG) genes, for example, extra sex combs. We also showed direct association of these factors with the repressive fragment, both in transgenic flies and in the context of the native mouse HoxD complex. These results suggest that the global repressive region of the HoxD complex functions in two very different species and that some PcG genes are involved in establishing the early repressive state of the HoxD complex, thus contributing to temporal colinearity.


Subject(s)
Body Patterning/genetics , Gene Expression Regulation, Developmental , Genes, Homeobox , Repressor Proteins/genetics , Repressor Proteins/physiology , Animals , Animals, Genetically Modified , Drosophila/embryology , Drosophila/genetics , Embryo, Mammalian , Embryo, Nonmammalian , Mice , Mice, Inbred C57BL , NIH 3T3 Cells , Polycomb Repressive Complex 2 , Polycomb-Group Proteins , Regulatory Sequences, Nucleic Acid/genetics , Repressor Proteins/metabolism , Transgenes
4.
J Biol Chem ; 279(26): 26868-75, 2004 Jun 25.
Article in English | MEDLINE | ID: mdl-15100221

ABSTRACT

We studied fibril formation in a family of peptides based on PHF6 (VQIVYK), a short peptide segment found in the microtubule binding region of tau protein. N-Acetylated peptides AcVYK-amide (AcVYK), AcIVYK-amide (AcPHF4), AcQIVYK-amide (AcPHF5), and AcV-QIVYK-amide (AcPHF6) rapidly formed straight filaments in the presence of 0.15 m NaCl, each composed of two laterally aligned protofilaments approximately 5 nm in width. X-ray fiber diffraction showed the omnipresent sharp 4.7-A reflection indicating that the scattering objects are likely elongated along the hydrogen-bonding direction in a cross-beta conformation, and Fourier transform IR suggested the peptide chains were in a parallel (AcVYK, AcPHF6) or antiparallel (AcPHF4, AcPHF5) beta-sheet configuration. The dipeptide N-acetyl-YK-amide (AcYK) formed globular structures approximately 200 nm to 1 microm in diameter. The polymerization rate, as measured by thioflavin S binding, increased with the length of the peptide going from AcYK --> AcPHF6, and peptides that aggregated most rapidly displayed CD spectra consistent with beta-sheet structure. There was a 3-fold decrease in rate when Val was substituted for Ile or Gln, nearly a 10-fold decrease when Ala was substituted for Tyr, and an increase in polymerization rate when Glu was substituted for Lys. Twisted filaments, composed of four laterally aligned protofilaments (9-19 nm width, approximately 90 nm half-periodicity), were formed by mixing AcPHF6 with AcVYK. Taken together these results suggest that the core of PHF6 is localized at VYK, and the interaction between small amphiphilic segments of tau may initiate nucleation and lead to filaments displaying paired helical filament morphology.


Subject(s)
Oligopeptides/chemistry , tau Proteins/chemistry , Amides/chemistry , Amino Acid Sequence , Buffers , Circular Dichroism , Kinetics , Microscopy, Electron , Morpholines/chemistry , Oligopeptides/genetics , Sodium Chloride/chemistry , Spectrometry, Fluorescence , Spectroscopy, Fourier Transform Infrared , X-Ray Diffraction , tau Proteins/genetics
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