Desloratadine citrate disodium versus epinastine for the treatment of chronic urticaria: a randomized controlled trial / 中华皮肤科杂志

Objective To evaluate the efficacy and safety of desloratadine citrate disodium versus epinastine for the treatment of chronic urticaria (CU).Methods A randomized,double-blind,double-dummy controlled clinical trial was conducted.Patients with CU were divided into test group and control group to be treated by oral desloratadine citrate disodium (8.8 mg/d) and epinastine (10 mg/d) respectively once a day for 28 days.All the patients were followed up after starting treatment.Therapeutic effect was evaluated,and adverse reactions were observed.Results One hundred and fifty-seven patients were enrolled in this study,and 142 patients were valid for evaluation of efficacy and safety at the end of study.After treatment for 28 days,there was no significant difference between the test group and control group in response rate (81.16 ％ vs.78.08 ％,P ＞ 0.05) or incidence rate of adverse reactions (13.89 ％ vs.12.16 ％,P＞ 0.05).Conclusion Desloratadine citrate disodium is effective and safe for the treatment of CU.

Construction, expression, purification and polyclonal antibody preparation of Fas extracellular region gene / 中国生化药物杂志

Purpose To construct expression vector of Fas extracellular region gene(eFas) ,to express and purify recombination protein and to prepare polyclonal antibody, which have laid a foundation of studying its function. Methods The eFas gene encoding sequence was acquired through overlapping PCR, and pET-22b ( + )/eFas expression vector was constructed. Then this vector was transformed into E. coli Rosetta-gami. Re-combinant protein was expression being induced by IPTG,and was purified using Ni-NTA matrix of affinity chromatograph. The purity of recombination protein was identified by SDS-PAGE. Hereafter, the purified eFas recombinant protein was immunized to New Zealand white rabbit in order to prepare polyclonal antibody. The titer of polyclonal antibody was determined by ELISA. Results The encoding sequence and expression vector of eFas was obtained while the interest protein was mainly expressed in the inclusion body. The eFas fusion protein's expression quantity accounts for more than 30% proportion of total E. coli protein. The eFas protein we obtained was provided with the purity of at least 95 % . Conclusion The successful constrution, expression and purification of FasL fusion protein and preparation of polyclonal antibody will provide some material for further studies of Fas.