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Two-Dimensional Electrophoretic Analysis of Soluble Leaf Proteins of a Salt-sensitive (Triticum aestivum) and a Salt-tolerant (T. durum) Cultivar in Response to NaCI Stress
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作者 Mustafa YILDIZ 《Journal of Integrative Plant Biology》 SCIE CAS CSCD 2007年第7期975-981,共7页
In this research, 3-day-old etiolated wheat seedlings of Triticum aestivum L. cv. Ceyhan-99 (salt-sensitive) and T. durum Desf. cv. Firat-93 (salt-tolerant) were grown in control and salt (150 mmol/L NaCl) treat... In this research, 3-day-old etiolated wheat seedlings of Triticum aestivum L. cv. Ceyhan-99 (salt-sensitive) and T. durum Desf. cv. Firat-93 (salt-tolerant) were grown in control and salt (150 mmol/L NaCl) treatments at a 15/25℃ temperature regime in the light for 12 days. Soluble proteins extracted from the first leaf tissues of two cultivars were analyzed by twodimensional (2-D) electrophoresis in order to detect NaCl-induced changes. The soluble leaf protein profiles of cultivars were observed to be similar. However, quantitative differences in 74 proteins were detected in the salt treatment group, compared to the control. Among the 74 protein spots, 14 were common for two cultivars. As a result of NaCl treatment, two low-molecular-weight (LMW) proteins (28.9 and 30.0 kDa) and one intermediate-molecular-weight (IMW) protein (44.3 kDa) in cv. Ceyhan-99 and six LMW proteins (18.6, 19.4, 25.7, 25.9, 26 and 27.6 kDa) in cv. Firat-93 were newly synthesized. The newly synthesized proteins were specific to each cultivar. In the Firat-93 cultivar, four proteins with LMW (24.8-27.9 kDa) were completely lost in NaCl treatment. Moreover, these four protein spots were not observed in both protein profiles of cv. Ceyhan-99. Most of these proteins were in acidic character (pl 〈6.0-6.9) and low molecular weight (〈31.6 kDa). It is suggested that the newly synthesized or completely lost LMW proteins may be important for cultivars differing in sensitivity towards NaCl. 展开更多
关键词 NaCl stress soluble leaf proteins Triticum aestivum Triticum durum two-dimensional electrophoretic analysis.
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An Eco-Friendly Wood Adhesive from Alfalfa Leaf Protein
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作者 Bengang Zhang Xuedong Xi +3 位作者 Zhigang Wu Hong Lei Lifen Li Meifen Tian 《Journal of Renewable Materials》 SCIE EI 2020年第11期1429-1441,共13页
According to the preparation method commonly used for soy proteinαbased adhesives,alfalfa leaf protein was used as the raw material to prepare alfalfa leaf protein-based wood adhesive.Differential scanning calorimetr... According to the preparation method commonly used for soy proteinαbased adhesives,alfalfa leaf protein was used as the raw material to prepare alfalfa leaf protein-based wood adhesive.Differential scanning calorimetry analyzer(DSC),X-ray diffraction(XRD)and Fourier transform infrared spectroscopy(FTαIR)were used to characterize properties of the alfalfa leaf protein-based adhesive in this paper.The results revealed the following:(1)Chemical compositions and chemical structures of the alfalfa leaf protein were basically identical with those of the soy protein,both belonging to spherical proteins with the basis and potential for protein adhesives preparation,and spatial cross-linked network structures would be easily formed.(2)Alfalfa leaf protein and soy protein adhesives had the similar curing behaviors,curing temperature of alfalfa leaf protein-based adhesive was relaαtively lower,and the heating rate had minor influence on curing temperature of alfalfa leaf protein-based adhesive.At different heating rates,change tendencies of curing reaction degrees of both the two adhesives were not totally the same.(3)Activation energy and reaction frequency factor of the alfalfa leaf protein-based adhesive were higher than those of soy protein-based adhesive,indicating that the curing reaction of the alfalfa leaf protein adhesive was more difficult than soy protein-based adhesive,thus the dry shear strength and water resistance of alfalfa protein-based adhesive were lower than those of soy protein-based adhesive.Dynamics models of curing reactions of alfalfa leaf protein-based adhesive and soy protein-based adhesive are dα=dt/1.06×10^(13)e^(-97370/RT)(1-α)^(0.938) and dα/dt=1.09×10^(11)e^(-84260/RT) 1-α)^(0.928) respectively.The results of this study will expand the selection of raw materials for protein-based wood adhesives. 展开更多
关键词 Alfalfa leaf protein wood adhesive curing properties thermal performance
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Effects of 4PU-30 on leaf senescence and degration of protein and nucleic acid in rice 被引量:1
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作者 TANG Risheng,MEI Chuangsheng,and WU Guangnam,Inst of Agrobiological Genetics and Physiotogy,Jiangsa Aoad of Agri Sci,Nanjing 210014,China 《Chinese Rice Research Newsletter》 1995年第4期8-9,共2页
4PU—30[N—phenyl—’N—(2—chloro—4—pyridyl) urea] is a new type of plant growth regulator with cytokinin properties. It has been confirmed to delay rice leaf senescence effectively. In order to elucidate the physi... 4PU—30[N—phenyl—’N—(2—chloro—4—pyridyl) urea] is a new type of plant growth regulator with cytokinin properties. It has been confirmed to delay rice leaf senescence effectively. In order to elucidate the physiological role of 4PU—30 in delaying senescence, the changes of protein, nucleic acid contents, and the related activities of degradative enzymes were studied. Shanyou 63, an indica hybrid rice was used for this experiment. In the in vitro experiment, two full—developed leaves from the top during heading stage were collected and cut into 5.0cm segments, They were floated on the surface of distilled water containing 0.1mg/14PU—30 and incubated in darkness at 30 C. The leaves floated on distilled water were used as control.It was observed that chlorophyll content in controlled leaves declined rapidly started from the second day and dropped by 93.4% on the 6th day while that in leaves treated with 4PU—30 declined by 41.4% only. During senescence, specific activities of hemoglobin—digesting 展开更多
关键词 PU ACID Effects of 4PU-30 on leaf senescence and degration of protein and nucleic acid in rice
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