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Chemical Compound Review:

RB45_SIGMA 1-amino-4-[[3-[(4,6-dichloro- 1,3,5-triazin...

Synonyms: R2507_SIGMA, R8754_SIGMA, NSC-364368, LS-20372, NSC364368, ...

Alderton, W.K. et al., Small, D.A. et al., Youn, H.J. et al., Nash, D.C. et al., Khan, A.A. et al.

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High impact information on Procion Brilliant Blue MX-R

A dye ligand (Procion Blue MX-R) has been covalently attached to PVA-PSDVB matrix and the lysozyme capacities of the PVA-PSDVB matrix have been determined [1].
Recombinant ricin A chain was irreversibly modified by Procion blue MX-R, a dichlorotriazinyl analogue of Cibacron blue F3G-A, at pH 7.5 and 4 degrees C in 90 h with over 95% loss of activity in an in vitro translation assay [2].
Quantitatively modified ricin A chain contained 2 mol Procion blue MX-R/mol 29-kDa subunit [2].
These spectral effects were observed both in the direct association of the Ru-HSA with Reactive Blue 4-labeled antibody, and in a competitive assay format wherein unlabeled HSA competed with Ru-HSA for the binding sites on the antibody [3].
The maximum decolorization was found at pH 3.0 and 4.0 in case of Reactive Blue 4 and Reactive Orange 86, respectively [4].

Associations of Procion Brilliant Blue MX-R with other chemical compounds

Horse liver alcohol dehydrogenase is irreversibly inactivated by Procion blue MX-R, a dichlorotriazinyl structural analogue of Cibacron blue F3G-A, with over 90% loss of activity within 30 min at pH 8.5 and 37 degrees C at a reactive dye concentration of 1 mM and enzyme subunit concentration of 5 microM [5].

References

Modification of polystyrenic matrices for the purification of proteins. Effect of the adsorption of poly(vinyl alcohol) on the characteristics of poly(styrene-divinylbenzene) beads for use in affinity chromatography. Nash, D.C., McCreath, G.E., Chase, H.A. Journal of chromatography. A. (1997) [Pubmed]
Affinity labeling of recombinant ricin A chain with Procion blue MX-R. Alderton, W.K., Thatcher, D., Lowe, C.R. Eur. J. Biochem. (1995) [Pubmed]
Fluorescence energy transfer immunoassay based on a long-lifetime luminescent metal-ligand complex. Youn, H.J., Terpetschnig, E., Szmacinski, H., Lakowicz, J.R. Anal. Biochem. (1995) [Pubmed]
Decolorization and removal of textile and non-textile dyes from polluted wastewater and dyeing effluent by using potato (Solanum tuberosum) soluble and immobilized polyphenol oxidase. Khan, A.A., Husain, Q. Bioresour. Technol. (2007) [Pubmed]
Affinity labelling of enzymes with triazine dyes. Isolation of a peptide in the catalytic domain of horse-liver alcohol dehydrogenase using Procion blue MX-R as a structural probe. Small, D.A., Lowe, C.R., Atkinson, T., Bruton, C.J. Eur. J. Biochem. (1982) [Pubmed]

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