1.Social alienation of survivors of nasopharyngeal cancer and its influencing factors
Yi ZHOU ; Li YANG ; Qiuting LIANG ; Xialan YE ; Yanxin ZHANG ; Jiayan LI
Chinese Journal of Practical Nursing 2023;39(1):59-64
Objective:To explore the status of social alienation among survivors of nasopharyngeal carcinoma and analyze its influencing factors.Methods:This study was a cross-sectional study. From October 2021 to January 2022, 200 survivors of nasopharyngeal carcinoma reviewed in the radiotherapy department of the First Affiliated Hospital of Guangxi Medical University were investigated by General Data Questionnaire, General Alienation Scale (GAS), Cancer Fatigue Scale (CFS) and Self-Perceived Burden Scale (SPBS).Results:The total score of GAS in survivors of nasopharyngeal carcinoma was (37.47 ± 2.88) points. The total scores of GAS were positively correlated with the total score and each dimension score of CFS and SPBS ( r values were 0.312-0.524, all P<0.01). Multivariable linear regression showed that the duration of diagnosis, whether or not having hearing loss, the number of symptoms, cancer fatigue and self-perceived burden were the main influencing factors of social alienation in survivors of nasopharyngeal carcinoma( t values were -3.99-4.86, all P<0.05), which could explain 49% of the total variation. Conclusions:Clinical medical staff should attach importance to social alienation of surviors of nasopharyngeal carcinoma. More attention should be paid to patients with less than one year of diagnosis, a large number of symptoms and hearing loss, and targeted intervention should be conducted to reduce the degree of social alienation of patients and promote their integration into society.
2.Oligomerization triggered by foldon to enhance the catalytic efficiency of feruloyl esterase.
Lei ZHANG ; Linchao LEI ; Guangya ZHANG ; Xialan LI
Chinese Journal of Biotechnology 2019;35(5):816-826
A new method to express oligomerized feruloyl esterase (FAE) in Pichia pastoris GS115 to improve the catalytic efficiency was developed. It was realized by fusing the foldon domain at the C-terminus of FAE, and the fusion protein was purified by histidine tag. Fusion of the feruloyl esterase with the foldon domain resulted spontaneously forming a trimer FAE to improve the catalytic performance. The oligomerized FAE and monomeric FAE were obtained by purification. The apparent molecular weight of the oligomerized FAE was about 110 kDa, while the monomeric FAE about 40 kDa, and the optimum temperature of the oligomerized FAE was 50 °C, which is the same as the monomeric one. The optimal pH of the oligomerized FAE is 5.0, while the optimal pH of the monomer FAE is 6.0. When compared with the monomeric ones, the catalytic efficiency (kcat/Km) of the oligomerized FAE increased 7.57-folds. The catalytic constant (kcat) of the oligomerized FAE increased 3.42-folds. The oligomerized FAE induced by foldon have advantages in the catalytic performances, which represents a simple and effective enzyme-engineering tool. The method proposed here for improving the catalytic efficiency of FAE would have great potentials for improving the catalytic efficiency of other enzymes.
Carboxylic Ester Hydrolases
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metabolism
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Catalysis
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Molecular Weight
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Pichia
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genetics
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metabolism
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Polymerization
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Protein Engineering
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Substrate Specificity