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1.
Article in Chinese | WPRIM | ID: wpr-905147

ABSTRACT

Objective:To observe the effect of water-based pulmonary rehabilitation on stable chronic obstructive pulmonary disease (COPD). Methods:From February, 2020 to February, 2021, 50 patients with stable COPD in our hospital were divided into control group (n = 25) and experimental group (n = 25), who accepted pulmonary rehabilitation training on land and in water, for eight weeks. They were measured forced expiratory volume in first second (FEV1), percents of forced expiratory volume in first second for prediction (FEVl%) and ratio of forced expiratory volume in first second in forced vital capacity (FEV1/FVC) with pulmonary function instrument; measured root mean square (RMS) of electromyogram of diaphragm and right transversus abdominis with surface electromyography; and assessed with modified breathlessness measurement of British Medical Research Council (mMRC), 6-minute walk test (6MWT) and quality of life scale for COPD adults (COPD-QOL) before and after treatment. Results:FEV1, FEVl%, FEV1/FVC, RMS of diaphragm and transversus abdominis, and 6MWT distance and COPD-QOL score increased in both group (t > 2.08, P < 0.05), and increased more in the experimental group than in the control group (t > 2.27, P < 0.05); while mMRC score decreased (t > 2.09, P < 0.05), and decreased more in the experimental group than in the control group (t = 2.13, P < 0.05). Conclusion:Water-based pulmonary rehabilitation training can further improve lung function, strength of respiratory muscles, dyspnea, tolerance and quality of life for patients with COPD.

2.
Chinese Journal of Biotechnology ; (12): 218-222, 2007.
Article in Chinese | WPRIM | ID: wpr-325390

ABSTRACT

<p><b>UNLABELLED</b>To prepare a novel fusion protein (tTF/SA) as a universal effector for targeting therapy of blood coagulation and to analyze its biological activities. The fusion gene tTF/SA was constructed by PCR, then inserted into expression vector pET22 b (+), and expressed in E. coli BL21 (DE3). The fusion protein was purified using Nickel-affinity chromatography column. The activities of tTF moiety of the fusion protein were analyzed by clotting assay and FX activation assay, and the binding activities of Streptavidin(SA) to Biotin(B) were analyzed using ELISA.</p><p><b>RESULTS</b>The recombinant plasmid tTF/SA/pET22 b (+) with the correct sequence was obtained. The fusion gene tTF/SA was expressed with high yield in E. coli BL21 (DE3). The purified fusion protein retain the abilities of activating FX, inducing blood coagulation, and binding Biotin. The fusion gene tTF/SA was successfully expressed in E. coli BL21 (DE3). The recombinant tTF/SA proteins retain the activities of TF and SA. The multitarget therapy of selectively inducing thrombosis in tumor blood vessels can be achieved by the combination of tTF/SA, as a universal effector, and biotinlated carriers directing to tumor blood vessels.</p>


Subject(s)
Animals , Mice , Binding, Competitive , Biotin , Metabolism , Blood Coagulation , Physiology , Chromatography, Affinity , Electrophoresis, Polyacrylamide Gel , Escherichia coli , Genetics , Gene Expression , Polymerase Chain Reaction , Recombinant Fusion Proteins , Genetics , Metabolism , Pharmacology , Streptavidin , Genetics , Metabolism , Pharmacology , Thromboplastin , Genetics , Metabolism , Pharmacology , Time Factors
3.
Chinese Journal of Biotechnology ; (12): 409-412, 2007.
Article in Chinese | WPRIM | ID: wpr-328014

ABSTRACT

To develop a new fusion protein (RGD)3/tTF for the therapy of the selective thrombosis of tumor blood vessels. The fused gene (RGD) 3/tTF was reconstructed by PCR, was cloned into vector pET22 b(+), and expressed in E. coli BL21 (DE3). The fusion protein was purified through Nickel-affinity chromatography column. The tTF activity of the fusion protein was detected by clotting assay and F X activation assay. The specific binding of (RGD) 3/tTF to alphavbeta3 was analyzed by indirect ELISA. The recombinant plasmid pET22 b(+)/(RGD)3/tTF was obtained and expressed in E. coli BL21 (DE3). The purified fusion protein could induce blood coagulation, activiate F X. The ability of (RGD) 3/tTF binding specifically to alphavbeta3 was increased by 32%, compared with RGD/tTF. A new fusion protein (RGD) 3/tTF was successfully expressed in E. coli BL21 (DE3). The expressed proteins retained tTF activity and showed a higher binding to alphavbeta3 than that of RGD/tTF.


Subject(s)
Animals , Humans , Mice , Blood Coagulation , Chromatography, Affinity , Dose-Response Relationship, Drug , Electrophoresis, Polyacrylamide Gel , Enzyme-Linked Immunosorbent Assay , Escherichia coli , Genetics , Factor Xa , Metabolism , Gene Expression , Integrin alphaVbeta3 , Metabolism , Oligopeptides , Genetics , Metabolism , Polymerase Chain Reaction , Protein Binding , Recombinant Fusion Proteins , Genetics , Metabolism , Pharmacology , Thromboplastin , Genetics , Metabolism
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