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The protease-catalyzed, kinetically controlled synthesis of a precursor dipeptide of thymopentin(TP-5), Z-Arg-Lys-NH2 in organic solvents was studied. Z-Arg-OMe was used as the acyl donor and Lys-NH2 was used as the nucleophile. An industrial alkaline protease alcalase and trypsin were used to catalyze the synthesis of the target dipeptide in water-organic cosolvent systems. The conditions of the synthesis reaction were optimized by examining the effects of several factors, including organic solvents, water content, temperature, pH, and reaction time on the yield of Z-Arg-Lys-NH2. The optimum conditions using alcalase as the catalyst are pH 10.0, 35 degrees C, in acetonitrile/DMF/Na2CO3-NaHCO3 buffer system (80:10:10, V/V), 6 h, with the dipeptide yield of 71.1%. Compared with alcalase, the optimum conditions for trypsin are pH 8.0, 35 degrees C, in ethanol/Tris-HCl buffer system (80:20, V/V), 4 h, with the dipeptide yield of 76.1%.

Yaowu Shengwu Jishu

Study on purification of recombinant bovine basic fibroblast growth factor

作者: Qu, Hongyan ; Feng, Xiuping ; Yang, Qian ; Yang, Hongcun

Purification of bFGF that is manufactured with E. coli by heparin affinity chromatog. was studied.Through SDS-PAGE and HPLC anal., its purity is 99.3% and 100% resp.Mol. weight is 17.8ku.Average relative activity is 2.8/10⁶AU/mg, its expressed quantity is 97.5 mg/mL.

Zhongguo Shenghua Yaowu Zazhi

Study on lyophilized recombinant basic fibroblast growth factor protective agent without human serum albumin

作者: Li, Shijun ; Ma, Yujie ; Lian, Guifeng ; Li, Rui ; Shi, Jing

Use of different combination of dextran and mannitol and glycine and gelatin as protective agents for recombinant basic fibroblast growth factor was studied.Results showed that some combination worked well as protective agents without human serum albumin.It was conclusion that the new protective agents could replace human serum albumin completely to protect lyophilized recombinant bFGF products.

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