Results 281 to 290 of about 14,424 (294)
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Hydrophobic chromatography of β‐galactosidase
Biotechnology and Bioengineering, 1980AbstractThe hydrophobic interaction of β‐galactosidase with Sepharose 4B substituted with 3,3′‐diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations.
R. G. Carbonell +2 more
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Galactosidases from Aspergillus niger
Archives of Biochemistry and Biophysics, 1970Abstract α- And β- d -galactopyranosidases were purified from a commercial crude enzyme preparation (Rhozyme HP-150). Although both enzymes were still not homogeneous, they were free of other possibly interfering glycosidases. Properties of the purified enzymes were studied.
Victoria Wacek, Yuan C. Lee
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Beta-Galactosidase Staining in the Skeleton
2014The lacZ gene, encoding for the β-galactosidase enzyme, is widely used as a reporter gene in bone biology due to the ease of visualization in situ on whole-mount or on tissue sections. In this protocol we provide detailed methods for visualizing this reporter gene for both in vivo and in vitro studies.
Jian Q. Feng, X. L. Han
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Cold Spring Harbor Protocols, 2010
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
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INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
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Biochemistry of -galactosidases.
Advances in enzymology and related areas of molecular biology, 1972J. B. Pridham, P. M. Dey
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Effects of exogenous β-galactosidase on cultured fibroblasts with β-galactosidase deficiency
Clinica Chimica Acta, 1987Shigeyuki Fukui +4 more
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1977
Publisher Summary β -Galactosidase of Escherichia coli (MW 540,000) is a tetramer of dentical subunits; it is obtained pure but is not of uniform activity. The highest reported activity is 910 units/mg. The evidence from affinity labeling of enzyme of intermediate activity (427 units/mg) by N-bromoacetylgalactosy lamine and its subsequent ...
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Publisher Summary β -Galactosidase of Escherichia coli (MW 540,000) is a tetramer of dentical subunits; it is obtained pure but is not of uniform activity. The highest reported activity is 910 units/mg. The evidence from affinity labeling of enzyme of intermediate activity (427 units/mg) by N-bromoacetylgalactosy lamine and its subsequent ...
openaire +2 more sources