Objective To evaluate the effect of infiltration anesthesia at Calot's triangle on postoperative analgesia in the patients undergoing laparoscopic cholecystectomy.Methods One hundred and forty patients,aged 18-64 yr,with 18 kg/m2 ≤ body mass index ≤ 31 kg/m2,of ASA physical status Ⅰ or Ⅱ,scheduled for elective laparoscopic cholecystectomy,were randomly divided into 2 groups (n =70 each):control group (group A) and infiltration anesthesia at Calot's triangle group (group B).In group B,1％ ropivacaine 10 ml was injected into Calot's triangle before dissection of the gallbladder,while the equal volume of normal saline was injected into Calot's triangle in group A.The patients in both groups received patient-controlled intravenous analgesia (PCIA) for 48 h starting from 10 min before the end of surgery.The VAS score was maintained below 4 during PCIA.When VAS score ≥ 4,lasting for more than 30 min,tramadol 1.5 mg/kg was injected intravenously.The consumption of physic liquor for PCIA,and requirement for tramadol were recorded.The incidence of puncture-related damage to Calot's triangle and local anesthetic intoxication and adverse effects such as nausea and vomiting within 48 h after surgery were also recorded.The first postoperative flatus time was recorded.Results Compared with group A,the consumption of physic liquor for PCIA,requirement for tramadol,and consumption of tramadol were significantly reduced,and no significant change was found in the incidence of nausea and vomiting and the first postoperative flatus time in group B.No puncture-related damage to Calot's triangle occurred in A and B groups.There was no local anesthetic intoxication in group B.Conclusion Infiltration anesthesia at Calot's triangle can optimize postoperative analgesia in the patients undergoing laparoscopic cholecystectomy.

This study was intended to establish a method of purification of HPV16 L1 protein expressed in a prokaryotic system and to obtain the purified protein. The prokaryotic expression vector pGEX-4T-1-HPV16 L1 was constructed and transformed into E. coli BL21 cell, and induced by 1 mM IPTG to express HPV16L1 protein. The inclusion bodies were isolated and solubilized with 8 M urea. After the urea was removed by gradual dialysis, the denatured L1 protein were renatured and then were purified by affinity chromatography. The results showed that HPV16L1 protein formed inclusion bodies in bacterial expression system, suggesting that this assay can be used to purify HPV16L1 protein and hence provide a basis for studying the applications of HPV16 L1 protein.
Capsid Proteins ; biosynthesis ; Escherichia coli ; metabolism ; Genetic Vectors ; Human papillomavirus 16 ; Oncogene Proteins, Viral ; biosynthesis