Chimeric rpoC'- lacZ' gene of the recombinant pUC19 plasmid reserving the β-galactosidase activity in Escherichia coli cells
نویسندگان
چکیده
منابع مشابه
Expression Cloning of Recombinant Escherichia coli lacZ Genes Encoding Cytoplasmic and Nuclear P-galactosidase Variants
Objective(s) Nonviral vector can be an attractive alternative to gene delivery in experimental study. In spite of some advantages in comparison with the viral vectors, there are still some limitations for efficiency of gene delivery in nonviral vectors. To determine the effective expression, the recombinant Escherichia coli lacZ genes were cloned into the different variants of pcDNA3.1 and the...
متن کاملExpression Cloning of Recombinant Escherichia coli lacZ Genes Encoding Cytoplasmic and Nuclear β-galactosidase Variants
OBJECTIVES Nonviral vector can be an attractive alternative to gene delivery in experimental study. In spite of some advantages in comparison with the viral vectors, there are still some limitations for efficiency of gene delivery in nonviral vectors. To determine the effective expression, the recombinant Escherichia coli lacZ genes were cloned into the different variants of pcDNA3.1 and then t...
متن کاملexpression cloning of recombinant escherichia coli lacz genes encoding cytoplasmic and nuclear p-galactosidase variants
objective(s) nonviral vector can be an attractive alternative to gene delivery in experimental study. in spite of some advantages in comparison with the viral vectors, there are still some limitations for efficiency of gene delivery in nonviral vectors. to determine the effective expression, the recombinant escherichia coli lacz genes were cloned into the different variants of pcdna3.1 and then...
متن کاملRegulation of enzymatic activity in the intact cell: the beta-D-galactosidase of Escherichia coli.
Large differences in enzymatic activity are often found between intact cells and extracts. Lacking a better explanation, it has frequently been assumed that the penetration of the substrate is the rate limiting step in the intact cells. The experiments reported here were designed to test several hypotheses which might account for the discrepancy. The 3-galactosidase (lactase) in Escherichia col...
متن کاملThe necessity of magnesium cation for acid assistance aglycone departure in catalysis by Escherichia coli (lacZ) beta-galactosidase.
1. Removal of Mg2+ from Escherichia coli (lacZ) beta-galactosidase slightly increases the rate of hydrolysis of galactosyl pyridinium salts, but decreases the rate of hydrolysis of arylgalactosides. 2. Fair correlation of logkcat. and log (Km) with the pKa of aglycone is now observed for arglygalactosides, as well as for glycosyl pyridinium salts. 3. Degalactosylation of Mg2+-free enzyme is the...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 1987
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.0001fd