One-step purification of hybrid proteins which have β-galactosidase activity
- 1 July 1984
- Vol. 29 (1-2), 27-31
- https://doi.org/10.1016/0378-1119(84)90162-8
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Point mutations that reduce the expression of malPQ, a positively controlled operon of Escherichia coliJournal of Molecular Biology, 1984
- Identification of the Escherichia coli cya gene product as authentic adenylate cyclaseJournal of Molecular Biology, 1984
- Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and MuJournal of Molecular Biology, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Lac repressor can be fused to β-galactosidaseNature, 1974
- The Purification of β-Galactosidase from Escherichia coli by Affinity ChromatographyPublished by Elsevier ,1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- On the subunit structure of wild-type versus complemented β-galactosidase of Escherichia coliJournal of Molecular Biology, 1968
- Délétions fusionnant ľopéron lactose et un opéron purine chez Escherichia coliJournal of Molecular Biology, 1965
- The genetic control and cytoplasmic expression of “Inducibility” in the synthesis of β-galactosidase by E. coliJournal of Molecular Biology, 1959