ObjectiveTo explore the application of discharge planning model in Respiratory Department. MethodWe developed discharge planning model in the Respiratory Department and performed standardized management on inpatients by assessing, planning, implementing and following up the whole process. A total of 716 discharged patients before the implementation of the planning model (January to March 2014) were designated as the control group, and 739 discharged patients after the model implementation (April to June 2014) were regarded as the observation group. Then, we compared such indexes as the rate of discharge planning, average length of hospital stay, retention rate of discharged patients, the number of new hospital admissions and medical orders during the time of weak nurse strength, and inpatient satisfaction before and after the model implementation. ResultsAfter implementation of discharge planning model, all observed indicators were significantly better in the observation group (P<0.05). ConclusionsImplementation of discharge planning model can effectively promote physician-nurse cooperation, plan health guidance for discharged patients, make them be ready to return to society and family, improve patients' satisfaction, and achieve the aim of patient-oriented high quality care. Meanwhile, it also can shorten the average length of hospital stay, reduce orders during the time of weak strength. It can not only ensure the ward medical indexes, but is helpful to manage nursing schedule.
ObjectiveTo optimize HSP65-MUC1 fusion protein purification in pilot scale through protein purification techniques and identify the methods for biological activity detection. MethodsE. coli expressing HSP65-MUC1 was obtained by fermentation, then homogenized to obtain the supernatant. To acquire high-purity, high-quality HSP65-MUC1, the supernatant was treated with saturated ammonium sulfate, phenyl sepharose FF column and Q FF ion-exchange chromatography column purification. The expression of CD86 on the surface of DC cells treated with HSP65-MUC1 was determined with flow cytometry. ResultsE. coli containing pET28a-HSP65-MUC1 recombinant plasmid can effectively express target protein. A total of 413.7 mg of HSP65-MUC1 was obtained after 10 g of fermented cells was treated with saturated ammonium sulfate, phenyl sepharose FF column and Q FF ion-exchange chromatography column, and the purity was nearly 96%. Compared with negative control (10.13%±0.89%), purified HSP65-MUC1 could significantly improve the expression of CD86 on the surface of DC cells (29.98%±1.02%). ConclusionThe pilot scale production of purified HSP65-MUC1 has been effectively optimized, and the methods of its biological activity detection have been identified, which simultaneously provides the basis for clinical studies.