A small portion of the crude extract was used to purify the β-galactosidase to homogeneity by affinity chromatography using p-aminobenzyl 1-thio-β-d -galactopyranoside immobilized onto cross-linked 4% beaded agarose (Sigma), as previously described [27 (link)]. Steady-state kinetic data for the substrates lactose or oNPG were obtained at 30°C in 50 mM sodium phosphate buffer, pH 6.5, with concentrations ranging from 0 to 600 mM for lactose and from 0 to 22 mM for oNPG. The kinetic parameters were calculated using nonlinear regression, fitting the observed data to the Michaelis-Menten equation using SigmaPlot (SPSS, Chicago, IL).
Beaded agarose
Manufactured by Merck Group
Sourced in United Kingdom
4% beaded agarose is a laboratory product used as a support material in various chromatographic and electrophoretic techniques. It is a type of agarose gel that is formed into small beads, providing a porous structure for the separation and purification of biomolecules such as proteins, nucleic acids, and other macromolecules. The 4% concentration refers to the percentage of agarose present in the beads.
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Lab products found in correlation
3 protocols using beaded agarose
1
Purification and Kinetics of β-Galactosidase
2
Fetuin-Agarose Affinity Chromatography
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An Amersham chromatography column was packed at room temperature with a final bed volume of 8 ml of Fetuin-Agarose in solution with 0.5 M NaCl and immobilised on cross-linked 4% beaded agarose (Sigma-Aldrich Company Ltd, UK). Prior to use the column was equilibrated with 8 column volumes of phosphate buffered saline (PBS).
3
Purification and Kinetics of β-Galactosidase
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
A small portion of the crude extract was used to purify the β-galactosidase to homogeneity by affinity chromatography using p-aminobenzyl 1-thio-β-d -galactopyranoside immobilized onto cross-linked 4% beaded agarose (Sigma), as previously described [27 (link)]. Steady-state kinetic data for the substrates lactose or oNPG were obtained at 30°C in 50 mM sodium phosphate buffer, pH 6.5, with concentrations ranging from 0 to 600 mM for lactose and from 0 to 22 mM for oNPG. The kinetic parameters were calculated using nonlinear regression, fitting the observed data to the Michaelis-Menten equation using SigmaPlot (SPSS, Chicago, IL).
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