Objective To evaluate the efficacy and safety profile of S-1 combined with oxaliplatin L-OHP (SOX) in the treatment of locally advanced or metastatic colorectal cancer.Methods 70 patients with advanced or metastatic colorectal cancer were randomly divided into trial group (35 cases) and control group (35 cases).The trail group was administered with dose of 130 mg/m2 L-OHP,plus S-1 which was given orally with body surface area (BSA) (BSA＜1.25 m2,80 mg/d; BSA≥ 1.25 m2 and ＜1.5 m2,100 mg/d; BSA≥ 1.50 m2 and ＜1.8 m2,120 mg/d; BSA＞1.8 m2,140 mg/d).This schedule was repeated every 3 weeks.The control group treated by FOLFOX4 regimen (L-OHP was given on d1 with 80 mg/m2 through intravenous,leucovorin was intravenously on d1,2,with 200 mg/m2,5-Fu was intravenously injected on d1,2,with 400 mg/m2,and was administered intravenously 44 hours with 1 200 mg/m2 on d1).This schedule was repeated every 2 weeks.Results The total clinical effective rate had no significant difference in the trail group and control group (51.4 ％,18/35 vs 45.7 ％,16/35) (x2 =0.229,P =0.632).Toxicity,nausea and vomiting rate in the trail group were lower than those in the control group (48.5 ％,16/35 vs 71.4 ％,25/35,68.6 ％,24/35 vs 88.6 ％,31/35,P ＜ 0.05),but hand-foot syndrome and peripheral neurotoxicity rates had no significant difference between two groups (P ＞ 0.05).Weight increased significantly after chemotherapy treatment in the two groups (t =2.702 5,P =0.003 9).Conclusion SOX regimen is feasible and safe for advanced colorectal cancer.

Glucoamylase is a critical ingredient for saccharification in the starch decomposition, and widely used in food, pharmaceutical and fermentation industries. Glucoamylases are usually thermostable and have peak activities at high temperature, as required for the industrial process of glucose production. In this study, a glucoamylase gene belonging to the glycoside hydrolase (GH) family 15, Tlga15A, was cloned from Talaromyces leycettanus JCM12802, and successfully expressed in Pichia pastoris GS115. Recombinant glucoamylase TlGA showed optimal activities at pH 4.5 and 75 °C. The result of thermostability analysis showed that TlGA retained above 70% activity after incubating for 1 h at 65 °C, and 43% residual activity after 30 min at 70 °C. Moreover, TlGA had high resistance to most metal ions and chemical reagents tested. Various starch substrates could be hydrolyzed by TlGA, including soluble starch (255.6±15.3) U/mg, amylopectin (342.3±24.7) U/mg, glycogen (185.4±12.5) U/mg, dextrin (423.3±29.3) U/mg and pullulan (65.7±8.1) U/mg. The primary, secondary and tertiary structures of glucoamylase were further analyzed. The low ratio of Gly in the primary structure and low exposed nonpolarity solvent accessible surface in the tertiary structure may be the main reasons for TlGA's thermostability. These results show that TlGA is great promising for potential use in the commercial production of glucose syrups. Moreover, this research will provide knowledge and innovating ideas for the improvement of glucoamylase thermostability.
Cloning, Molecular ; Enzyme Stability ; Glucan 1,4-alpha-Glucosidase ; Hydrogen-Ion Concentration ; Pichia ; Talaromyces ; Temperature