Objective To observe the influence of dezocine used before end of operation on postoperative recovery and its inter-vention effect on postoperative pain in the patients with gynecological laparoscopic operation .Methods 60 patients(ASA Ⅰ - Ⅱ ) scheduled hysterectomy operation by gynecological laparoscopy were randomly divided into the observation group (dezocine group , n=30) and the control group(normal saline group ,n=30) .Remifentanil combined with propofol was intravenously given for con-ducting endotracheal intubation general anesthesia .The observation group was given dezocine 0 .1mg/kg(diluting to 10mL by nor-mal saline) at 30-40 min before the end of operation ,while the control group was given the same volume of physiological saline . Blood pressure ,heart rate(HR) ,recovery time ,adverse reactions during the recover period and postoperative pain before induction , after injection and before recovery were recorded .Results The elevation of mean arterial pressure(MAP) and the increase of HR during the recovery period in the observation group were lower than those in the control group (P<0 .05);the recovery time of au-tonomous respiration and extubation time had no statistical difference between the two groups (P>0 .05) .PO2 ,PCO2 and SaO2 had no statistical difference between the two groups (P>0 .05);the postoperative agitation-sedation scores(PASS) and the visual ana-logue scale(VAS) scores in the observation group were significantly lower than those in the control group (P<0 .05) ,and the oc-currence rate of chills also was lower than that in the control group (P<0 .05) .Conclusion Intravenous dezocine before the end of operation in the gynecological laparoscopic operation can effectively inhibit the cardiovascular stress reaction ,does not affect the re-covery speed ,moreover can decrease the restlessness during the recovery period and postoperative pain .

Objective To clone and express of Rv0091 encoding protein in Mycobacterium tuberculosis,identify and characterize of the enzyme activities.Methods Construct the Rv0091 prokaryotic expression plasmid,the vector was transformed into E.coli strain BL21trxB.After induced by IPTG,recombinant protein was purified by Ni2+-NTA chromatography and analyzed for purity by SDS-PAGE gels stained with Coomassie Blue.Immunological activity was identified by Western blot.The recombinant protein molecular weight was identified by Mass spectrometry.The enzyme-coupled assay detectes enzyme activity.Results The expression plasmid pET32a-Rv0091 was constructed and expressed in E.coli.BL21trxB,and the optimum expression system was conformed.The purity of the recombinant protein was more than 95％.Western blot analysis confirmed that recombinant protein was one of Mycobacterium tuberculosis proteins.Mass spectrometry identified the relative molecular weight and theoretical molecular weight was basically the same.Enzyme assay showed the recombinant protein able to catalyze the substrate MTA.Enzymatic properties showed that the optimal buffer for the phosphate and Hepes buffer,the poor thermal stability of the enzyme,the optimal temperature of 37℃,optimal pH10-12,when the pH ≤7,the protein denaturation and loss of some vitality.Conclusion The recombinant protein methylthioadenosine nucleosidase(MTAN) was obtained and enzyme activity was detected and plays a key role in the metabolism of Mycobacterium tuberculosis.