[Expression of somatostatin gene in E. coli D29A1].
Somatostatin gene fragment extracted and purified from plasmid pSom5 bacterium was ligated with the plasmid pBD2 DNA. Transformation of E. coli D29A1 with the chimeric plasmid DNA led to the synthesis of a polypeptide including the sequence of amino acids corresponding to somatostatin. The chimeric protein (50000 dalton) was purified and characterized by the beta-galactosidase affinity chromatography and the expression of the somatostatin gene in E. coli D29A1 is certain after the radioimmunoassay of the chimeric protein and its mixture by treatment with cyanogen bromide.
Zeng
Y X
YX
Division of Veterinary Immunology and Microbiology, Nanjing Agricultural University.
Du
N X
NX
Tan
J Y
JY
D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D008969:Molecular Sequence Data; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis; D013004:Somatostatin / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification
D011994:Recombinant Proteins; D013004:Somatostatin