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At least 1,063 records · Page 59Linked to original sources
PubMed1980

Triazine dyes, a new class of affinity labels for nucleotide-dependent enzymes.

A number of reactive dichlorotriazine dyes specifically and irreversibly inactivate pig heart lactate dehydrogenase, yeast glucose 6-phosphate dehydrogenase and yeast hexokinase at sites competitive with NAD+, NADP+, and ATP respectively. Monochlorotriazine dyes, including Cibacron Blue F3G-A, do not inactivate lactate dehydrogenase but display high affinity and thus inhibit the inactivation by dichlorotriazine dyes. These data are interpreted in terms of the ability of nucleotide-binding enzymes to bind polysulphonated aromatic chromophores.

Affinity Labels↗
PubMed1982

Metal-ion-promoted binding of triazine dyes to proteins. The interaction of Cibacron Blue F3G-A with yeast hexokinase.

Bivalent metal ions, particularly Zn2+ and other members of the first-row transition series, promote irreversible inactivation of yeast hexokinase by Cibacron Blue F3G-A at a site competitive with both ATP and D-glucose. Difference spectroscopy indicates that the protein-dye dissociation constant is decreased from 250 micrometers in the absence of metal ions to less than 100 micrometers in the presence of appropriate concentrations of metal ions, with specificity displayed in the sequence of Zn2+ greater than Cu2+ greater than Ni2+ greater than Mn2+. Quantitative inactivation of yeast hexokinase leads to the incorporation of approx. 1 mol of Cibacron Blue F3G-A/mol of subunit of mol. wt. 51 000 in both the presence and the absence of metal ion. These results suggest the formation of a highly specific ternary complex involving enzyme, dye and metal ion at the active-site region of the enzyme, and correlate well with the known effects of metal ions in promoting the binding of hexokinase to immobilized Cibacron Blue F3G-A.

Anthracenes↗
PubMed1999

Adhesive bonding of noble metal alloys with a triazine dithiol derivative primer and an adhesive resin.

The purpose of this study was to evaluate the bond strength and durability of a metal adhesive system bonded to noble metal alloys. Disc specimens were cast from type IV gold (type IV, Casting Gold M. C., metal-ceramic gold (Au-Pt-Pd, Degudent Universal, metal-ceramic palladium (Pd-Ga-Co, PTM 88 silver-indium (Ag-In-Zn, Salivan Hard and silver-palladium-copper-gold (Ag-Pd-Cu, S12) alloys and pure silver (pure Ag). The specimens were air-abraded with 50 micron alumina, conditioned with a thiol-based primer designed for noble alloys (V-Primer), and then bonded with an adhesive resin (Super-Bond Opaque Ivory). Shear bond strengths were determined after repeated thermocycling (4-60 degrees C, 1 min each, 100 000 cycles). The average bond strengths in MPa (n=8) were 30.9 for the type IV alloy, 29.0 for the Ag-Pd-Cu alloy, 28.0 for the Au-Pt-Pd alloy, 26.3 for the pure Ag, 26.0 for the Pd-Ga-Co alloy and 9.3 for the Ag-In-Zn alloy. The Ag-In-Zn alloy exhibited significantly lower bond strength than the other alloys, whereas the bond strengths of the other four alloys and pure Ag were comparable (P<0.05). It is concluded that the combined use of the thiol derivative primer and the adhesive resin is effective for bonding the noble metal alloys examined, with the exception of the Ag-In-Zn alloy.

Adhesives↗
PubMed1979

The binding of aminoacyl-tRNA synthetases to triazine dye conjugates.

The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.

Amino Acyl-tRNA Synthetases↗
PubMed1984

Studies on the nature of transition-metal-ion-mediated binding of triazine dyes to enzymes. The interaction of procion red MX-8B with carboxypeptidase G-2.

Several reactive azoic dichlorotriazinyl dyes specifically and irreversibly inactivate the folate-degrading enzyme carboxypeptidase G-2 at a site competitive with the enzyme substrates methotrexate (4-amino-N10-methylfolic acid) and p-aminobenzoyl-L-glutamate. Although the less reactive monochlorotriazinyl dye, Procion red H-8BN, is unable to inactivate the enzyme, it is capable of marked inhibition of inactivation by dichlorotriazinyl dyes in the presence of Zn2+. Zinc ions and, to a lesser extent other first row transition metal ions, significantly enhance the affinity of Procion red H-8BN and its analogues Procion red MX-8B and Procion red MX-2B, for carboxypeptidase G-2. It is proposed that this effect is mediated through the formation of a specific tetracoordinate Zn2+ complex between the azo linkage and adjacent sulphonate and hydroxyl functions of the dye and an appropriate ligand on the protein. Carboxypeptidase G-2 quantitatively inactivated with the dichlorotriazinyl dye, Procion red MX-8B, contains approximately 1 mol dye/mol subunit of Mr 42000. Proteolytic cleavage of the labelled enzyme and resolution of the peptides by reverse-phase high-performance liquid chromatography yields a principal red peptide which on amino acid sequence analysis results in the identification of the dye binding domain. The affinity label, Procion red MX-8B, is believed to be attached to the hydroxylic side chain of Thr-279.

Affinity Labels↗