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1.
Zhonghua Yi Xue Za Zhi ; 99(3): 178-182, 2019 Jan 15.
Article in Chinese | MEDLINE | ID: mdl-30669759

ABSTRACT

Objective: To analyze the 20-year survival rate, causes of death and predictors of systemic lupus erythematosus (SLE). Methods: A retrospective analysis was performed on 217 newly SLE patients who were diagnosed and treated by Peking University People's Hospital before June 2008. The clinical features and serologic data were studied. Survival rate of SLE patients over time, living conditions, causes of death and prognostic indicators of mortality were studied. Results: The 10-, 15-and 20-year cumulative survival rate was 90.3%,88.1%and 79.6%, respectively. Infection and lupus encephalopathy were the main causes of death. Cox regression analysis revealed that lupus nephritis, neuropsychiatric systemic lupus erythematosus and age at the diagnosis were independent risk determinants for mortality. Conclusion: Prognosis of SLE remains to be improved. Early diagnosis, control of SLE organ damage and infection prevention are critical to improve survival of SLE patients.


Subject(s)
Lupus Erythematosus, Systemic , Humans , Lupus Erythematosus, Systemic/epidemiology , Lupus Nephritis , Prognosis , Retrospective Studies , Risk Factors , Survival Analysis , Survival Rate
2.
Genet Mol Res ; 14(4): 15488-504, 2015 Dec 01.
Article in English | MEDLINE | ID: mdl-26634515

ABSTRACT

An antifungal protein exhibiting a high activity against Sclerotinia sclerotiorum in vivo was purified by ammonium sulfate precipitation, hydrophobic chromatography, and gel filtration chromatography from the culture filtrate of the endophytic Bacillus subtilis strain Em7. The protein was characterized as a ß-1,3-1,4-glucanase according to amino acid analysis, and showed excellent properties in thermal stability and acid resistance. At the same time, the antifungal protein was cloned and heterologously expressed in Escherichia coli BL21. The recombinant protein was purified and showed similar enzymatic properties to the native protein, exhibiting strong inhibitory activity against S. sclerotiorum. This shows that the ß-1,3-1,4-glucanase may play a very important role in B. subtilis Em7 biocontrol function. In addition, many physiochemical properties of the native and purified recombinant protein were compared, including the effect of pH, temperature, metal cations, substrate specificity, and kinetic parameters. All parameters were similar between the native and recombinant purified protein, indicating that the purified recombinant protein has potential for industrial applications.


Subject(s)
Antifungal Agents/pharmacology , Ascomycota/drug effects , Bacillus subtilis/genetics , Bacterial Proteins/genetics , Bacterial Proteins/pharmacology , Recombinant Proteins , Bacterial Proteins/chemistry , Bacterial Proteins/isolation & purification , Enzyme Activation , Escherichia coli/genetics , Escherichia coli/metabolism , Gene Expression , Kinetics , Microbial Sensitivity Tests , Protein Stability , Substrate Specificity
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