Protein contents in bacterial extracts were measured by the Coomassie G dye-binding method using a Bio-Rad prepared reagent.
Kuan et al. [24, 27] and Liew et al. [24, 27] also reported the same avidin-biotin binding method using gold-PSA-DNA probe conjugates.
The protein concentrations of intra- and extra-enzymes were determined by the Coomassie Brilliant Blue G250 binding method using bovine serum albumin solution to make standard curve [ 50].
One enzyme unit was defined as the amount of the laccase that oxidized 1 μmol of the ABTS substrate per min. Protein concentration in the enzymatic extracts was determined by the Coomassie Blue binding method using bovine serum albumin as the standard [ 39].
α-Amylase enzyme was immobilized on bioactive phospho-silicate glass (PS-glass) as a novel inorganic support by physical adsorption and covalent binding methods using glutaraldehyde and poly glutaraldehyde as a spacer.
Protein concentration was determined by the Bradford dye-binding method using the Bio-Rad protein assay reagent (Hercules, CA, USA).
The data were normalized to the total protein amounts in cell layers determined by the Bio-Rad protein assay (Bio-Rad Laboratories InCA, Hercules, CA), based on the Bradford dye-binding method, using BSA as standard.
Moreover, we confirmed the requirement of the glutamic acid residue in the C-terminal tail of the laminin γ1 chain, substitution of which with glutamine abolishes the integrin binding activity of LN511E824, in our culture method using an EQ mutant of rLN511E8.
To facilitate analysis of other sequences and additional data, we have developed an on-line web tool, ProbTF, which implements our probabilistic TF binding prediction method using multiple data sources.
GTPγS binding was measured using a filter binding method as described previously (Garcia-Marcos et al., 2010, 2011b).
