Polyamide 5,6 (PA 5,6) fibers were prepared using the melt-spinning method. The effects of draw ratio and temperature on the structure and properties of PA 5,6 fibers were investigated by means of differential scanning calorimetry (DSC), wide-angle X-ray diffraction, sonic velocity and tensile test measurements. DSC results revealed that the melting temperature showed no considerable variation, while the heat of fusion increased with increments with draw ratio and temperature. It was found that the crystallinity and crystal size of PA 5,6 fibers were directly proportional to the draw ratio and temperature and the orientation factor increases as expected upon drawing. The tenacity and Young's modulus were found to be increased, while the elongation at break decreased with the draw ratio and temperature. The improvement in mechanical properties may be attributed to the increase of orientation along the fiber axis and the crystallinity.
The non-isothermal crystallization behavior of polyamide 5,6 (PA56) was investigated by differential scanning calorimeter (DSC), and the non-isothermal crystallization kinetics were analyzed using the modified Avrami equation, the Ozawa model, and the method combining the Avrami and Ozawa equations. It was found that the Avrami method modified by Jeziorny could only describe the primary stage of non-isothermal crystallization kinetics of PA56, the Ozawa model failed to describe the nonisothermal crystallization of PA56, while the combined approach could successfully describe the non-isothermal crystallization process much more effectively. Kinetic parameters, such as the Avrami exponent, kinetic crystallization rate constant, relative degree of crystallinity, the crystallization enthalpy, and activation energy, were also determined for PA56.
This study was designed to use comparative proteomics technology to find the differentially expressed proteins between human lung adenocarcinoma and paired normal tumor-adjacent lung tissues. The total proteins of 20 human lung adenocarcinoma tissues and paired normal tumor-adjacent lung tissues were separated by means of immobilized pH gradient-based two-dimensional gel electrophoresis (2-DE) and Coomassie Blue staining. The differentially expressed proteins were analyzed with image analysis software and then identified by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) and quadrupole time of flight mass spectrometry (Q-TOF-MS/MS). (1) Well-resolved, highly reproducible 2-DE patterns of human lung adenocarcinoma and paired normal tumor adjacent lung tissues were obtained. (2) PDQUEST 2D image analysis software was used to analysis 20 cases of lung adenocarcinoma and paired normal lung tissues, 1006 +/- 54 spots were matched among tumor tissues and normal lung tissues. Twenty-eight differentially expressed spots were screened. (3) Twenty non-redundant differentially expressed proteins were identified by mass spectrometry, thirteen proteins were up-regulated, and seven proteins were down-regulated, some proteins were involved in the regulation of cell signal transduction or metabolized enzyme of cell. (4) To validate the results screened by proteome research, immunohistochemistry was used to validate several lung adenocarcinoma differentially expressed proteins including 14-3-3 sigma, annexin 1, and manganese superoxide dismutase. The results showed that these three proteins were really differentially expressed between lung adenocarcinoma and paired normal lung tissues. These results will provide scientific foundation and new clue for the research of human lung adenocarcinoma.
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