Tryptophan Photo-Oxidation by Clay-Adsorbed Sensitizers

AbstractThe photo-oxidation of tryptophan (TRP), photosensitized by methylene blue (MB) exchanged on hectorite, Wyoming bentonite and laponite is strongly influenced by three factors: (i) Fe(III) in the structure, which quenches the excited state of MB; (ii) the adsorption site of MB, as photo-oxidation only takes place with MB on the external surface; (iii) dye aggregation, which reduces the yield. Rose bengal (RB), chemically anchored on the external surface of Barasym does not sensitize the photo-oxidation of TRP.

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The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites

Biochemical Journal ◽

10.1042/bj1200151 ◽

1970 ◽

Vol 120 (1) ◽

pp. 151-157 ◽

Cited By ~ 30

Author(s):

M. S. Rose ◽

E. A. Lock

Keyword(s):

Amino Acids ◽

Methylene Blue ◽

Guinea Pig ◽

Rose Bengal ◽

Binding Sites ◽

Liver Protein ◽

Pig Liver ◽

Photo Oxidation ◽

Kinetics Of ◽

Guinea Pig Liver

A protein fraction was isolated from guinea-pig liver that binds triethyltin with an affinity of approx. 2×106m−1 at pH8.0. It was shown that the protein responsible for binding 70% of the triethyltin found in guinea-pig liver after injection of radioactively labelled triethyltin is at most a few per cent of the total liver protein. Evidence is presented from the kinetics of loss of binding and loss of certain amino acids on photo-oxidation with either Methylene Blue or Rose Bengal that each binding site consists of two histidine residues.

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The action of rennin on casein: the effect of modifying functional groups on the casein

Journal of Dairy Research ◽

10.1017/s0022029900018537 ◽

1965 ◽

Vol 32 (2) ◽

pp. 193-201 ◽

Cited By ~ 26

Author(s):

R. D. Hill ◽

Raione R. Laing

Keyword(s):

Methylene Blue ◽

Amino Acid ◽

Functional Groups ◽

Amino Acid Analysis ◽

Side Chains ◽

Photo Oxidation

Summaryk-Casein and whole casein when photo-oxidized in the presence of methylene blue lose the ability to clot when treated with rennin. Two effects are involved—first the photo-oxidation alters the k-casein fraction so that the rennin is unable to split off the glycopeptide fragment, and secondly, in whole casein the photo-oxidation interferes with the aggregation in the presence of Ca++that normally follows rennin action. As a result of amino acid analysis and specific treatments which affect other photo-oxidizable side chains, it is concluded that both of these effects are caused by the alteration of histidines.

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Biodegradation of Synthetic Dye by Endophytic Fungal Isolate in Calotropis procera Root

International Journal of Applied Sciences and Biotechnology ◽

10.3126/ijasbt.v3i3.13136 ◽

2015 ◽

Vol 3 (3) ◽

pp. 373-380 ◽

Cited By ~ 4

Author(s):

Shiv Kumar Verma ◽

Anand Kumar ◽

Moti Lal ◽

Mira Debnath

Keyword(s):

Methylene Blue ◽

Rose Bengal ◽

Dye Degradation ◽

Fungal Endophytes ◽

Brilliant Blue ◽

Calotropis Procera ◽

Methyl Red ◽

Coomassie Brilliant Blue ◽

Fungal Isolates ◽

Coomassie Brilliant

In this study, based on colony morphology characteristics, a total of 19 fungal endophytes were isolated from root of Calotropis Procera a traditional Indian medicinal plant. All fungal isolates were screened for their dye degradation ability. The dyes used as test dyes were Rose Bengal (RB), azo dye Methyl Red (MR), Coomassie Brilliant Blue (CBB) and Methylene Blue (MB) and the concentration of each dye in the experiment was kept 100mg/L. Among the 19 fungal endophytic isolates (CPR1-CPR19), only one isolate CPR4 showed strong dye decolourization capability against all the four test dye. Dye decolourization ability by the isolate CPR4 was determined to be 97.4%, 87%, 65% and 45% for Rose Bengal (RB), Methyl Red (MR), Coomassie Brilliant Blue (CBB) and Methylene Blue (MB) respectively. Complete colour decolourization was observed with rose Bengal followed by Methyl Red. Glucose minimal medium was used for liquid and solid culture of fungal isolates. Fungal biomass production in the presence of four test dye was studied and compare with control culture of fungal endophytes. Effect of temperature, pH, stationary and agitation conditions on dye degradation was also studied.Int J Appl Sci Biotechnol, Vol 3(3): 373-380

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Effect of reverse micelles on the Rose Bengal-sensitized photo-oxidation of 1- and 2-hydroxynaphthalenes

Redox Report ◽

10.1179/135100004225005165 ◽

2004 ◽

Vol 9 (4) ◽

pp. 199-205 ◽

Cited By ~ 6

Author(s):

Marta Luiz ◽

M. Alicia Biasutti ◽

Norman A. García

Keyword(s):

Rose Bengal ◽

Reverse Micelles ◽

Photo Oxidation ◽

The Rose

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Limited sensitivity of pigment photo-oxidation in isolated thylakoids to singlet excited state quenching in photosystem II antenna

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2006.08.017 ◽

2006 ◽

Vol 455 (1) ◽

pp. 77-88 ◽

Cited By ~ 14

Author(s):

Stefano Santabarbara

Keyword(s):

Excited State ◽

Photosystem Ii ◽

Singlet Excited State ◽

Photo Oxidation ◽

Excited State Quenching ◽

Limited Sensitivity

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The enzymic degradation of l-serine O-sulphate. Mechanism of the reaction

Biochemical Journal ◽

10.1042/bj1280041 ◽

1972 ◽

Vol 128 (1) ◽

pp. 41-46 ◽

Cited By ~ 5

Author(s):

N. Tudball ◽

P. Thomas

Keyword(s):

Hydrogen Atom ◽

Carbon Atom ◽

Rose Bengal ◽

Incubation Medium ◽

Tritiated Water ◽

Competitive Inhibitor ◽

Histidine Residues ◽

Photo Oxidation ◽

Rapid Inactivation ◽

Mechanism Of The Reaction

1. During the enzyme-catalysed degradation of l-serine O-sulphate no exchange occurs between the hydrogen atom attached to the α-carbon atom of the substrate and the tritiated water of the incubation medium. 2. The participation of an intermediate carbanion has been demonstrated in the degradation by performing the reaction in the presence of tetranitromethane. 3. Photo-oxidation of the enzyme in the presence of Rose Bengal led to a rapid inactivation of enzyme with the concomitant loss of four histidine residues/molecule. 4. Rose Bengal was also a non-competitive inhibitor of the enzyme.

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