Inhibition of xanthine oxidase by Caulerpenyne from Caulerpa prolifera

Cengiz, Sevilay; Çavaş, Levent; Yurdakoç, Mehmet; Aksu, Sevil

doi:10.5505/tjb.2012.98698

Cited by 14 publications

(8 citation statements)

References 37 publications

(66 reference statements)

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“…The crude product was purified from two silica gel column using the mixture of petroleum ether/ethyl acetate (7/3, v/v) and petroleum ether/diethyl ether (6/4, v/v) as eluents, respectively. Reverse phase HPLC and 1 H NMR spectroscopic analyses were conducted in order to check the purity of the CYN (Cengiz et al, 2009). The NMR data were identical with those reported in the literature (Amico et al , 1978).…”

Section: Isolation Of Cyn From C Proliferamentioning

confidence: 64%

Seasonal rubisco enzyme activities and caulerpenyne levels in invasive Caulerpa racemosa var. cylindracea and native Caulerpa prolifera

2012

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Caulerpa racemosa var.cylindracea (C.racemosa) is an invasive marine seaweed in the Mediterranean Sea. Since no valid eradication method has been existed in the scientific literature on this species, it has currently been continuing its invasion along the coastlines of 13 Mediterranean countries. One of the important factors responsible for its invasion is thought to be its toxic secondary metabolite, i. e. caulerpenyne (CYN). The present paper investigates seasonal changes in the secondary metabolite CYN and rubisco enzyme (EC 4.1.1.39) activities of invasive C. racemosa and native C. prolifera. Inasmuch as no correlation between CYN level and rubisco enzymic activity was observed in these species, it is considered that the regulation of CYN synthesis and rubisco enzymic activity might be controlled independently. In conclusion, the further analysis on the rubisco enzymic activity determinations with methyl-erythritol-4-phosphate and mevalonate pathways considered to be responsible for CYN bio-synthesis in invasive and native Caulerpa species in the Mediterranean Sea and these subjects should be studied in great detail to get the overall picture.

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Section: Isolation Of Cyn From C Proliferamentioning

confidence: 64%

Seasonal rubisco enzyme activities and caulerpenyne levels in invasive Caulerpa racemosa var. cylindracea and native Caulerpa prolifera

2012

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“…Kong et al [18] was reported the condition of similar pH. As for the other different measurement conditions, it was reported by CeCngiz et al [8], that is, at a temperature of 37°C and pH 9.0. The differences in the optimum conditions for the measurement of temperature and substrate concentration are caused by different methods, tools and measurement time.…”

Section: Inhibitory Assay Of the Extract Against Xomentioning

confidence: 90%

“…Therefore, optimization of XO activity was done to study the effects of these parameters on XO activity. Optimized parameters include temperature (25-35°C), pH [6][7][8][9], and substrate concentrations (0.10-1.00 mM). Based on those contours (data not shown), the optimum conditions for each of the parameter temperature, pH and xanthine concentration was 30°C, pH 7.5, and 1.00 mM.…”

Section: Inhibitory Assay Of the Extract Against Xomentioning

confidence: 99%

“…Luteolin and quercetin were reported to follow the competitive inhibition against XO [5]. A noncompetitive inhibition of XO, among others, is indicated by Fraxinus angustifolia leaf extract [6] and Tephrosia purpurea root extract [7], while the caulerpenyne (CYN) from the extract of Caulerpa prolifera was reported to show the uncompetitive inhibition [8].…”

Section: Introductionmentioning

confidence: 99%

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Inhibition Kinetics of <i>Sida rhombifolia</i> L. Extract Toward Xanthine Oxidase by Electrochemical Method

Iswantini¹,

Yulian²,

Mulijani³

et al. 2014

Indones. J. Chem.

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Sida rhombifolia L. is a traditional medicinal plant that has been known with potential as antigout. The previous research suggested that flavonoids crude extract of S. rhombifolia had an inhibitory activity toward xanthine oxidase by 71% and a spectrophotometric measurement showed that the type of flavonoids crude extract inhibition was a competitive inhibition. The purpose of the research was to investigate the type of inhibition kinetic of S. Rhombifolia's ethanol extract by electrochemical method and to compare the measurements of linearity and sensitivity between spectrophotometric and electrochemical methods. The results showed that the yield of S. Rhombifolia's ethanol extract was 9.82% with the inhibitory activity ranging from 13.64% to 82. 69% (5.00-200 mg L -1 ). Kata Kunci: kinetika inhibisi; Sida rhombifolia L.; xantina oksidase; elektrokimia

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“…Following up reports on the inhibitory activity of CYN ( 1 ) on microtubule protein polymerization, first synthetic CYN analogues in form of colchicine hybrids were generated, however with limited activity 3. CYN ( 1 ) itself is also active as inhibitor of telomerase,4 amylase,5 xanthine oxidase6 and plant lipoxygenases (LOs) 7. We reported that CYN ( 1 ) inhibits soybean LO with an IC 50 value of 5.1 μ M in an uncompetitive manner 7b.…”

Section: Methodsmentioning

confidence: 99%

Photoredox Catalysis of Intramolecular Cyclizations with a Reusable Silica‐Bound Ruthenium Complex

et al. 2015

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Photoredox catalysis with the use of a stable, reusable silica‐bound chromophore was applied to the intramolecular cyclization of a series of 2‐benzylidenehydrazinecarbothioamides to give 5‐phenyl‐1,3,4‐thiadiazol‐2‐amines. The catalyst was readily prepared by carbodiimide‐mediated coupling of commercially available amine‐functionalized silica beads to a carboxylic acid functionalized ruthenium complex. The immobilized catalyst was readily removed from the reaction product by filtration and was used eight times without loss of catalytic activity. This simple, safe, and practical method is an attractive alternative to conventional procedures.

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Inhibition of xanthine oxidase by Caulerpenyne from Caulerpa prolifera

Cited by 14 publications

References 37 publications

Seasonal rubisco enzyme activities and caulerpenyne levels in invasive Caulerpa racemosa var. cylindracea and native Caulerpa prolifera

Seasonal rubisco enzyme activities and caulerpenyne levels in invasive Caulerpa racemosa var. cylindracea and native Caulerpa prolifera

Inhibition Kinetics of <i>Sida rhombifolia</i> L. Extract Toward Xanthine Oxidase by Electrochemical Method

Photoredox Catalysis of Intramolecular Cyclizations with a Reusable Silica‐Bound Ruthenium Complex

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