Distinction between cofactor-dependent and-independent phosphoglycerate mutases by chromatography on Cibacron Blue-Sepharose

1983 ◽  
Vol 3 (9) ◽  
pp. 857-861 ◽  
Author(s):  
Nicholas C. Price ◽  
Evelyn Stevens
Keyword(s):  
Cibacron Blue ◽  
Blue Sepharose

The binding of phosphoglycerate mutases from a variety of sources to Cibacron Blue-Sepharose has been examined. Those enzymes which are dependent on 2,3-bisphosphoglycerate (BPG) for activity bind to the immobilized dye and can be eluted by BPG. Those enzymes which are independent of BPG do not bind to the immobilized dye. The possible structural signifi-cance of this distinction is discussed.

scholarly journals The interaction of anthraquinone dyes with the plasmid-mediated OXA-2 β-lactamase

1982 ◽  
Vol 205 (2) ◽  
pp. 413-417 ◽  
Author(s):  
C Monaghan ◽  
S Holland ◽  
J W Dale
Keyword(s):  
Specific Effect ◽  
Nucleotide Binding ◽  
Red Shift ◽  
Side Chain ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Cibacron Blue ◽  
Anthraquinone Dyes ◽  
Cibacron Blue 3Ga ◽  
Blue Sepharose

Although beta-lactamases do not require any nucleotide co-substrates, the OXA-2 type is inhibited competitively by Cibacron Blue 3GA, and by other anthraquinone dyes, including some simpler compounds with no side chain. The enzyme causes a red shift in the spectrum of Cibacron Blue. The beta-lactamase can be adsorbed in Blue Sepharose and specifically eluted by benzylpenicillin. These results indicate that the binding of anthraquinone dyes is a specific effect similar to that seen with many nucleotide-binding enzymes.

Purification of human α-2-macroglobulin by chromatography on Cibacron Blue Sepharose

1978 ◽  
Vol 89 (1) ◽  
pp. 274-278 ◽  
Author(s):  
G.D. Virca ◽  
J. Travis ◽  
P.K. Hall ◽  
R.C. Roberts
Keyword(s):  
Cibacron Blue ◽  
Blue Sepharose

Purification of diphtheria toxin by chromatography on Cibacron Blue-Sepharose

1983 ◽  
Vol 39 (8) ◽  
pp. 885-886 ◽  
Author(s):  
G. Antoni ◽  
M. Bigio ◽  
G. Borri ◽  
M. C. Casagli ◽  
P. Neri
Keyword(s):  
Diphtheria Toxin ◽  
Cibacron Blue ◽  
Blue Sepharose

scholarly journals Isolation of albumin from whole human plasma and fractionation of albumin-depleted plasma

1976 ◽  
Vol 157 (2) ◽  
pp. 301-306 ◽  
Author(s):  
J Travis ◽  
J Bowen ◽  
D Tewksbury ◽  
D Johnson ◽  
R Pannell
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Affinity Column ◽  
Plasma Albumin ◽  
Cibacron Blue ◽  
Blue Sepharose

The dye Cibacron Blue F-3-GA was conjugated to Sepharose to provide an affinity column for serum albumin. Passage of whole human plasma through a column of Cibacron Blue-Sepharose results in the removal of approx. 98% of the albumin. The latter can be quantitatively recovered by desorption with NaSCN. Albumin-depleted plasma can be readily resolved into discrete fractions by a combination of conventional biochemical techniques. In particular, the resolution of plasma proteins with properties similar to those of native human plasma albumin can readily be accomplished by ion-exchange chromatography of the Sepharose-dye-treated plasma on DEAE-cellulose.

Purification of d-amino acid oxidase apoenzyme by affinity chromatography on Cibacron Blue Sepharose

1985 ◽  
Vol 347 ◽  
pp. 316-319 ◽  
Author(s):  
Joëlle Léonil ◽  
Sylvie Langrené ◽  
Sames Sicsic ◽  
François Le Goffic
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Cibacron Blue ◽  
Blue Sepharose

scholarly journals Inhibition of monkey liver serine hydroxymethyltransferase by Cibacron Blue 3G-A

1980 ◽  
Vol 187 (1) ◽  
pp. 249-252 ◽  
Author(s):  
K S Ramesh ◽  
N Appaji Rao
Keyword(s):  
Absorption Spectrum ◽  
Binding Domain ◽  
Serine Hydroxymethyltransferase ◽  
Free Enzyme ◽  
Cibacron Blue ◽  
Monkey Liver ◽  
Dye Absorption ◽  
Blue Sepharose

Cibacron Blue 3G-A inhibited monkey liver serine hydroxymethyltransferase competitively with respect to tetrahydrofolate and non-competitively with respect to L-serine. NADH, a positive heterotropic effector, failed to protect the enzymes against inhibition by the dye and was unable to desorb the enzyme from Blue Sepharose CL-6B gel matrix. The binding of the dye to the free enzyme was confirmed by changes in the dye absorption spectrum. The results indicate that the dye probably binds at the tetrahydrofolate-binding domain of the enzyme, rather than at the ‘dinucleotide fold’.

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