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1.
J Inorg Biochem ; 105(7): 966-71, 2011 Jul.
Article in English | MEDLINE | ID: mdl-21549660

ABSTRACT

Root border cells (RBCs) and their secreted mucilage are suggested to participate in the resistance against toxic metal cations, including aluminum (Al), in the rhizosphere. However, the mechanisms by which the individual cell populations respond to Al and their role in Al resistance still remain unclear. In this research, the response and tolerance of RBCs to Al toxicity were investigated in the root tips of two soybean cultivars [Zhechun No. 2 (Al-tolerant cultivar) and Huachun No. 18 (Al-sensitive cultivar)]. Al inhibited root elongation and increased pectin methylesterase (PME) activity in the root tip. Removal of RBCs from the root tips resulted in a more severe inhibition of root elongation, especially in Huachun No. 18. Increasing Al levels and treatment time decreased the relative percent viability of RBCs in situ and in vitro in both soybean cultivars. Al application significantly increased mucilage layer thickness around the detached RBCs of both cultivars. Additionally, a significantly higher relative percent cell viability of attached and detached RBCs and thicker mucilage layers were observed in Zhechun No. 2. The higher viability of attached and detached RBCs, as well as the thickening of the mucilage layer in separated RBCs, suggest that RBCs play an important role in protecting root apices from Al toxicity.


Subject(s)
Aluminum/pharmacology , Glycine max/drug effects , Plant Roots/drug effects , Seedlings/drug effects , Carboxylic Ester Hydrolases/metabolism , Cell Survival/drug effects , Cells, Cultured , Enzyme Assays , Plant Roots/cytology , Plant Roots/growth & development , Rhizosphere , Seedlings/cytology , Seedlings/growth & development , Glycine max/cytology , Glycine max/growth & development
2.
J Fluoresc ; 18(2): 573-9, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18157619

ABSTRACT

When 1.00 mol l(-1) I(-) is used as ion perturber, rhodamine 6G (Rh 6G) can emit strong and stable room temperature phosphorescence (RTP) on filter paper substrate in KHC(8)H(4)O(4)-HCl buffer solution (pH = 3.50), heated at 70 degrees C for 10 min. NaIO(4) can oxidize Rh 6G, which makes the RTP signal quench. Terbutaline sulfate (TBS) can inhibit NaIO(4) from oxidizing Rh 6G, which makes the RTP signal of Rh 6G enhance sharply. The content of TBS is linear correlation to DeltaIp of the system. Based on the facts above, a new inhibition solid substrate-room temperature phosphorimetry (SS-RTP) for the determination of trace TBS has been established. The linear range of this method is 0.0104-2.08 pg spot(-1) (corresponding concentration: 0.026-5.2 ng ml(-1), with a sample volume of 0.4 microl) with a detection limit (L.D.) of 2.6 fg spot(-1) (corresponding concentration: 6.5 x 10(-12) g ml(-1)), and the regression equation of working curve is DeltaIp = 2.040 + 54.54 m(TBS) (pg spot(-1)), n = 6, correlation coefficient is 0.9994. For the samples containing 0.0104 pg spot(-1) and 2.08 pg spot(-1) TBS, the relative standard deviation (RSD) are 3.8% and 2.3% (n = 8), respectively, indicating good precision. This method has been applied to determination of trace TBS in the practical samples with satisfactory results. The reaction mechanism of NaIO(4) oxidizing Rh 6G to inhibit SS-RTP for the determination of trace TBS is also discussed.


Subject(s)
Luminescent Measurements/methods , Periodic Acid/pharmacology , Rhodamines/chemistry , Terbutaline/analysis , Oxidation-Reduction , Spectrometry, Fluorescence , Temperature
3.
Zhongguo Ying Yong Sheng Li Xue Za Zhi ; 21(4): 367-70, 2005 Nov.
Article in Chinese | MEDLINE | ID: mdl-21180148

ABSTRACT

AIM: To detect effect of the different frequency of chronic electrical stimulation (CES) on myofibrillar isoform, myosin heavy chain (MHC) and metabolic enzyme activities. METHODS: The histochemical method and SDS-polyacrylamide gel electrophoresis were respectively employed. RESULTS: (1)There were a significant increase in I myo-fibrillar isoform and I MHC isoform and decrease in II B myofibrillar isoform and II B MHC isoforms in the chronic low frequency electrical stimulation (CLFES) 10 Hz and 20 Hz groups, but opposite results were found in the chronic high frequency electrical stimulation (CHFES) 50 Hz and 100 Hz groups. (2) There were a significant increase in the aerobic-oxidative enzyme activities and capacity, and a concomitant significant drop in glycolysis enzyme activities in CLFES groups, but opposite results were found in CHFES 50 Hz and 100 Hz groups. CONCLUSION: It was suggested that there was a significant dependent relation between chronic electrical stimulation frequency and myofibrilla isoforms, myosin heavy chain (MHC) and metabolic enzyme activities.


Subject(s)
Adaptation, Physiological , Diaphragm/metabolism , Diaphragm/physiology , Electric Stimulation , Myosin Heavy Chains/metabolism , Nonmuscle Myosin Type IIB/metabolism , Animals , Diaphragm/enzymology , Muscle Contraction , Protein Isoforms , Rabbits
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