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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of China Medical University is the property of Journal of China Medical University Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

To explore the effect of a chitosan-based preservative solution (10 mg/mL chitosan + 5 mg/mL tea polyphenol + 2 000 U/mL lysozyme) on the change in the muscle proteome of grass carp during cold storage, differential proteomic analysis of fresh fish and nine-day-stored fish with or without (control) preservative treatment was conducted by two-dimensional electrophoresis-mass spectrometry (2DE-MS). The results showed that the 2DE map of the preservative-treated group was not obviously different from that of the fresh group, except for a decrease in the abundance of fast troponin T and an increase in the abundance of slow troponin T and adenylate kinase isoenzyme. However, the 2DE profile of the control group differed greatly from that of the fresh group in both the number and signal intensity of protein spots. Further analysis showed that the abundance of fast troponin T, tropomodulin 4, synaptopodin 2 and pyruvate kinase type M were down-regulated, while the abundance of myosin heavy chain, myosin light chain 1, α-actin, α-tropomyosin and intermediate light meromyosin were up-regulated. Moreover, compared with the preservative-treated group, the abundance of three troponins T were decreased, while the abundance of myosin heavy chain, intermediate light meromyosin, α-actin, α-tropomyosin and creatine kinase M-type were increased in the control group, suggesting that creatine kinase could serve as an indicator for evaluating grass carp muscle spoilage. This study demonstrates that the chitosan-based composite preservative can maintain the stability of grass carp muscle protein during cold storage.

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objectives Proteomics principles and techniques were used to detect and screen out the expression of differential proteins in urine of athletes after exercise with different intensities; the changes of urinary protein components and the correlations among the changes, human immune function and exercise fatigue were investigated, which provided scientific basis and practical methods for exercise biochemical monitoring. Methods Based on Two-dimensional electrophoresis (2-DE), differential expression of urine proteome of 8 male athletes was analyzed after exercises of 55%, 75%, 85% and 95% VO2max intensity, respectively; the protein expressed levels which were up-regulated by at least 5-fold and with repeatability were screened and analyzed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Results A total of 275 differentially expressed protein points was detected after different exercise intensities, down-regulated protein points were 85 and up-regulated 190. After screening expressed levels which were up-regulated by at least 5-fold protein, a total of 29 protein was identified, showing a close relation to the biological processes of immune regulation and inflammatory response. Conclusions Proteomics better explains what happens to the urine proteome after different exercises, among which, apolipoprotein and zinc-a2-glycoprotein are related to lipid metabolism after exercise; immunoglobulin, albumin, complement component C3, mannose-binding lectin protein 19 and Vitamin D binding protein are related to immune regulation. The theoretical basis and application method are provided for the evaluation of the effects of exercise training on human immune function and fatigue. [ABSTRACT FROM AUTHOR]

[Objective] In this study, we would search for the differentially expressed protein between the rapeseed addition line EE and rapeseed inoculated with the root-knot nematode by proteomic technique to screen the resistance-related protein against root-knot nematodes. [Method] Roots of the the resistant rapeseed addition line EE and susceptible rapeseed were used as materials. Differentially expressed proteins were screened by proteomic two-dimensional electrophoresis and Image Master 5. 0 software. Proteins were identified by MALDl-TOFTOF/ MS mass spectrometry. In addition, functional classification, metabolic pathway analysis, subcellular localization and proteins interaction analysis of identified proteins were carried using Gene Ontology, KEGG, WoLF PSORT and STRING. [Result] Madara and rapeseed addition line EE had 1184 and 1163 protein spots, respectively. 21 differentially expressed proteins were successfully identified by MALDlTOF/ TOF MS. Among these proteins, more than half of them were localized extracellularly (52. 38 %), followed by cytoplasm (28. 57 %), chloroplasts (4. 76 %), mitochondria (4. 76 %), and internal plasma reticulum (4. 76 %), vacuoles (4. 76 %). Analysis of protein interactions showed that endogenous a-amylase/ subtilisin inhibitors was connected wisth 3-isopropylmalate dehydratase large subunits, tubulin a-6 chain, epidermis-specific secreted glycoprotein EPl, BnaC04g03560D and BnaC06g34210D. [ Conclusion]The screened resistance-related proteins lay the foundation for cloning of resistance genes and breeding of new resistant varieties with molecular markers in future. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Edulis Fungi is the property of Acta Edulis Fungi and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Forest Research is the property of Forest Research Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of China Brewing is the property of China Brewing Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Two-dimensional electrophoresis (2-DE) is an important technology in proteomics research. The experiment of the effect of heat shock treatment on the expression profile of bacterial protein was designed to provide undergraduate an experiment for 2-DE technique. The soluble proteins from Escherichia coli was studied by 2-DE. The higher stability and resolution repeatability 2-DE maps were obtained. Through this experiment，students can master the basic principle， experiment method of 2-DE and the general idea of protein extraction. [ABSTRACT FROM AUTHOR]

The purpose of the study was to develop 2-DE method suitable for Mango leaf proteome analysis in future. This study compared TCA-Acetone protocol, Phenol Extraction-Ammonium Acetate Precipitation method( PE-AP) and Optimized Protocol of Phenol ExtractionAmmonium Acetate Precipitation( OPE-AP) to examine their effectiveness on protein extraction of mango leaf tissue. The result indicates that OPE-AP gained better quality of protein than PE-AP. The optimization on the steps of washing and drying of the pellet can effectively improve the quality of protein extracted by TCA-Acetone protocol. The p H value of extraction buffer applied in OPE-AP can greatly affect protein yield, number of protein spots and their distribution on 2-DE gel. Proteins extracted by extraction buffer with p H 8. 5 result in the most number of 2-DE protein spots, but the protein spot resolution in the zone of small molecular weigh is lower than proteins extracted by p H9. 0 extraction buffer. Proteins extracted by TCA-Acetone protocol have lower protein spot resolution in the zone of high molecular weigh than proteins extracted by OPE-AP, but gain much higher protein resolution in zones where proteins have small molecular weigh and high value of isoelectric point than the latter one. There is a high complementary result in protein spot resolution between protocol of TCA-Acetone and OPE-AP, thus their combination can be applied in two-dimensional electrophoresis to improve protein resolution. [ABSTRACT FROM AUTHOR]

Objective To establish two-dimensional electrophoresis (2-DE) technology for hydatid fluid of the parasite Echinococcus granulosus. Methods We extracted total proteins of Echinococcus granulosus by lyophilization and studied the changes of 2-DE picture under different methods of dealing with the protein samples, pH range of IPG strip and quantitative loading of the samples. Results The two-dimensional collection of illustrative plate with better resolution and repetition was achieved when the hydatid fluid dealt with ReadyPrepTM 2-D Cleanup Kit was analyzed using 400 μg of quantitative loading and IPG strips pH 7-10. Conclusion The established 2-DE method and maps of hydatid fluid of the parasite Echinococcus granulosus can provide theoretical evidence for proteomic study of Echinococcus granulosus. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Oil Crop Sciences is the property of Oil Crops Research Institute of Chinese Academy of Agricultural Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

In order to explore the cadmium (Cd)鄄tolerance mechanism of rice (Oryza sativa), a hydroponic experiment with Cd鄄tolerant rice cultivar PI312777 and Cd鄄sensitive rice cultivar IR24 was conducted. The cultivars were treated with 0 (control), 50, and 100 滋mol·L-1 of Cd2+ for 7 days, and the differential expression of proteins in their leaves were analyzed by two鄄dimensional electrophoresis and MALDI鄄TOF/ MS approach. Under Cd stress, 31 protein spots in PI312777 leaves and 19 protein spots in IR24 leaves had significantly different expression, compared with the control. In PI312777 leaves, the 24 of 31 proteins had 4 proteins related to photosynthesis, 11 proteins related to cell metabolism and defense, 3 proteins related to other metabolism pathway, and 2 proteins were unknown proteins; in IR24 leaves, the 15 of 19 proteins were identified. Under Cd鄄stress, the heat shock protein, glutathione鄄diulfide reductase, poteasome subunit alpha type鄄6,1,6鄄bisphosphate aldolase, thioredoxin, and DNA repair鄄recombination protein in PI312777 leaves were up鄄regulated expressed, while these proteins in IR24 were not significantly changed except the down鄄regulation of 1,6鄄bisphosphate aldolase and thioredoxin. The higher Cd鄄tolerance of PI312777 could have close relations with the differentially expressed proteins. [ABSTRACT FROM AUTHOR]

By using two-dimensional electrophoresis and mass spectrometry techniques, the proteomes in the tillering node of cold-resistant winter wheat Dongnongdongmai 1 and cold-susceptible winter wheat Jimai 22 before and after low temperature treatment were comparatively analyzed. It was observed that within the range of pH 4-7, there was a significant difference in the expression level of 55 protein spots in the protein profiles of tillering node before and after low temperature treatment, and 47 of the 55 protein spots were expressed in the two cultivars. After low temperature treatment, the abundance value of 23 protein spots increased, with the absolute abundance being higher in Dongnongdongmai 1 than in Jimai 22, while that of 7 protein spots decreased, with the absolute abundance being lower in Dongnongdongmai 1 than in Jimai 22. The expression level of 8 protein spots specific in Dongnongdongmai 1 was up-regulated. In all of the up-regulated proteins, their expression level in Dongnongdongmai 1 was 2.1 - 16.5 times as high as that in Jimai 22, among which, 10 protein spots had an expression level of 4 times high. In the down-regulated proteins, their expression level in Dongnongdongmai 1 was 0.1-0.4 times as high as that in Jimai 22. The differential protein spots were detected by mass spectrometry, and identified by compared with retrieval database. A total of 51 protein spots fingerprints were obtained, among which, 15.7% were of stress protein, 27.5% were of metabolism-related protein, 19.6% were signaling molecules, 9.8% were of unknown protein, and other proteins took up 27.4%. These variously expressed proteins might play an important role in the cold resistance of Dongnongdongmai 1. [ABSTRACT FROM AUTHOR]

In order to find the insect-resistant composition and differentially expressed proteins of mungbean, Jinlv No.7, B20 and Weilv 2117 were used as experimental materials, and the differential proteins and functions of mungbean varieties that are resistant and susceptible to bruchids were compared and analyzed by two dimensional gel electrophoresis (2-DE) and identified by mass spectrometry. Among the samples, 15 protein spots showed a more than 2.5 times reproducible up-regulated, significance 6 of them were successfully identified by the database, and involved three kinds of proteins. They are the alpha and beta subtype 8S globulin, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBis CO) subunits binding protein and the precursor peptide chains for amylase inhibitor and trypsin inhibitor. The protein expressions of B49 (alpha subtype 8S globulin) and B31 (RuBis CO subunits binding protein) of insect-resistant mungbean were 10 000 and 23 times higher than that of insect-susceptible mungbeans. It stunted the growth and even death of the Callosobruchus chinensis L. that alpha and beta subtype 8S globulin and RuBis CO subunits binding protein and precursor peptide chains for amylase inhibitor and trypsin inhibitor of insect-resistant mungbean, the bruchid resistance effect of these three proteins need to further verified in terms of the quantity and the combined effect.

Molting fluid, a liquid between the old epidermis and new epidermis, plays an important role in the process of ecdysis and metamorphosis for insect. In order to explore the function of molting fluid, we used two-dimensional electrophoresis to study the molting fluid during the prepupal stage and pre-eclosion stage. More than 200 protein spots were found in the molting fluid of the 2 stages, which distributed in the 4-9 of pI and 10-180 kDa of molecular weight. We selected 42 spots to be analyzed by the matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF/TOF) from the molting fluid of pre-eclosion stage, of which 34 proteins were identified successfully, including apolipoprotein, protease and protease inhibitors, chitin-binding protein and protein involved in immunity. Some of the proteins demonstrated differential expression between the two stages of metamorphosis. In order to validate the result from proteomics analysis, we studied expression of the apolipoprotein D by Q-PCR from the developmental stages. The results showed that the gene encoding apolipoprotein D had the high expression from the 1st day to the 4th day of the pupa stage, which indicated they could be involved in eclosion due to the abundant accumulation in the late pupa. Our results offered more clues for understanding the mechanism of ecdysis and metamorphosis in insect and could give reference for further study of molting fluid.