scholarly journals The sensitivity of carthamin and safflor yellow B colours towards redox substances

2014 ◽  
Vol 62 (1-2) ◽  
pp. 25-31 ◽  
Author(s):  
Koshi Saito ◽  
Makiko Matsumura ◽  
Mihoko Takahashi

The sensitivities of carthamin and safflor yellow B towards oxidants and antioxidants were compared in bufferized solutions at various given concentrations. The test chemicals affected variously on the pigment colourations: (1) externally charged 0<sub>2</sub> had less effect on the colour change of carthamin, (2) organe-yellow coloured safflor yellow B was bleached by the gas flush, (3) carthamin showed little or no affinitive property for H<sub>2</sub>0<sub>2</sub> at 0.001-230 µM level, (4) safflor yellow B reacted positively with the oxidant and was changed readily to faint yellow unknown compounds, (5) double-faced responses could be found in carthamin solution with L-ascorbic acid or with D-isoascorbic acid, namely the former antioxidant intensified the colour of carthamin and the latter reduced the red colouration, (6) hydroquinone emphasized the red colour of carthamin in solution, (7) safflor yellow B shifted bathochromically in hydroquinone containing solution, however, it showed no shift in L-ascorbic acid and D-isoascorbic acid solutions. The data are discussed from the standpoint of oxidative dissimilation of the quinochalconoids in the floral tissues of dyer's saffron capitula.

1943 ◽  
Vol 20 (11) ◽  
pp. 224-226 ◽  
Author(s):  
Daniel Swern ◽  
A. J. Stirton ◽  
J. Turer ◽  
P. A. Wells

1971 ◽  
Vol 22 (10) ◽  
pp. 540-542 ◽  
Author(s):  
F. E. Huelin ◽  
I. M. Coggiola ◽  
G. S. Sidhu ◽  
H. Kennett

2021 ◽  
Vol 1033 ◽  
pp. 77-81
Author(s):  
Li Ping Tu ◽  
Guo Wei Xu

By fixing Quantum Dots (QDs) on gold electrodes with dithiol compounds, a novel Ascorbic Acid sensor without any redox mediator was desighed. First, the fabrication process of sensor was described.Sencond, the characteristics of the sensor were investigated. Third,the sensor was tested in Ascorbic Acid solutions of different concentrations.From the results,it shows that the performance of photoelectrochemical sensor were influenced by the bias voltage and the amplitude of photocurrent changed with the Ascorbic Acid concentration linearly in detection range.


1995 ◽  
Vol 268 (6) ◽  
pp. C1430-C1439 ◽  
Author(s):  
R. T. Franceschi ◽  
J. X. Wilson ◽  
S. J. Dixon

Ascorbic acid is necessary for expression of the osteoblast phenotype. We examined whether Na(+)-dependent transport is required for MC3T3-E1 preosteoblast cells to respond to vitamin C and investigated the role of membrane transport in the intracellular accumulation and function of ascorbate. MC3T3-E1 cells were found to possess a saturable, stereoselective, Na(+)-dependent ascorbic acid transport activity that is sensitive to the transport inhibitors sulfinpyrazone, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, and phloretin. Transport activity showed no competition with glucose or 2-deoxyglucose and was not inhibited by cytochalasin B, indicating that it is distinct from known hexose transporters. On addition of 100 microM ascorbic acid to the extracellular medium, intracellular concentrations of 10 mM were reached within 5-10 h and remained constant for up to 24 h. A good correlation was observed between intracellular ascorbic acid concentration and rate of hydroxyproline synthesis. Although ascorbic acid was transported preferentially compared with D-isoascorbic acid, both isomers had equivalent activity in stimulating hydroxyproline formation once they entered cells. Marked stereoselectivity for extracellular L-ascorbic acid relative to D-isoascorbic acid was also seen when alkaline phosphatase and total hydroxyproline were measured after 6 days in culture. Moreover, ascorbic acid transport inhibitors that prevented intracellular accumulation of vitamin blocked the synthesis of hydroxyproline. Thus Na(+)-dependent ascorbic acid transport is required for MC3T3-E1 cells to achieve the millimolar intracellular vitamin C concentrations necessary for maximal prolyl hydroxylase activity and expression of the osteoblast phenotype.


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