An improved procedure using ferricyanide for detecting catalase isozymes

Woodbury, W.; Spencer, A. K.; Stahmann, Mark A.

doi:10.1016/0003-2697(71)90375-7

Cited by 625 publications

(286 citation statements)

References 5 publications

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“…In the enzyme assays, H 2 O 2 was used as the substrate for CAT (assay pH 7.0), indophenyl acetate for EST (assay pH 5.5), p-nitrophenyl phosphate for ACP (assay pH 5.2), orthodianisidine for POD (assay pH 6.0), o-catechol for PPO (assay pH 6.8), and diethylenetriamine pentaacetic acid, nitroblue tetrazolium and xanthine for SOD (pH 7.8). The isoenzyme profiles of CAT (Woodbury et al, 1971), EST (Brewbaker et al, 1968), ACP (Murray and Collier, 1977), POD (Sheen and Calvert, 1969), PPO (De Ascensao and Dubery, 2000) and SOD (Chen and Pan, 1996) were examined by native PAGE. Each experiment was replicated five times.…”

Section: Methodsmentioning

confidence: 99%

Alterations in biochemical components in mesta plants infected with yellow vein mosaic disease

Chatterjee

Ghosh

2008

Braz. J. Plant Physiol.

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ALTERATIONS IN BIOCHEMICAL COMPONENTS IN MESTA PLANTS:Yellow vein mosaic disease of mesta (kenaf, Hibiscus cannabinus L.; and roselle, H. sabdariffa L.) is a new entrant to the disease scenario and it is associated with a novel monopartite Begomovirus. Changes in different biochemical parameters in diseased mesta plants were observed as compared to healthy ones. Isozyme pattern and assays of different enzymes, namely catalase, acid phosphatase, peroxidase, esterase, polyphenol oxidase and superoxide dismutase, revealed lower activities of catalase, acid phosphatase and peroxidase enzymes and enhanced activities of esterase, polyphenol oxidase and superoxide dismutase in diseased plants as compared to healthy ones. Due to the infection, chlorophyll content, phenolics and total soluble protein decreased whereas free amino acid, proline and disease-related proteins increased in the host plants. Differential responses of polyacetylene and isoflavone content as well as SDS-PAGE band profiling of total soluble proteins were also observed in plants due to the infection.

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Section: Methodsmentioning

confidence: 99%

Alterations in biochemical components in mesta plants infected with yellow vein mosaic disease

Chatterjee

Ghosh

2008

Braz. J. Plant Physiol.

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“…For CAT activity, gels were rinsed with double distilled water and then incubated in a solution of H 2 O 2 (0.010%; v/v) for 20 min. Following a brief rinse with water, the gels were incubated in 1% ferric chloride and 1% potassium ferricyanide solution for 15 min, respectively for detection of CAT bands (Woodbury et al, 1971). …”

Section: Sds-page Native Page and Activity Staining (In-gel Assay)mentioning

confidence: 99%

Cold stress affects antioxidative response and accumulation of medicinally important withanolides in Withania somnifera (L.) Dunal

Mir

Khazir

et al. 2015

Industrial Crops and Products

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Withania somnifera (L.) Dunal (Indian ginseng) is a high value medicinal plant. It synthesizes a large array of biologically active withanolides. In this study, two month old seedlings of AGB002 (wild genotype) and AGB025 (cultivated genotype) of W. somnifera were subjected to cold stress (4 • C) under controlled envi-ronment. Plants were analyzed for three medicinally important secondary metabolites (withanolide A, withanone and withaferin A), lipid peroxidation (MDA), cell injury, superoxide radical (O 2 •− ) accumula-tion and anti-oxidative enzymes activities such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX) and glutathione reductase (GR). Increases in the titers of superoxide anion and MDA were observed from day 1 to day 7 in both genotypes, although the increase on the first day of exposure was significantly higher. Enzymatic activities of SOD, CAT, APX and GR also showed an increasing trend in both genotypes and reached a maximum on day 7 of the cold temperature exposure; however, this increase was higher in AGB002 than AGB025. Withanolide A (WS-1) in the roots of both genotypes sig-nificantly decreased on the first day of cold exposure and then showed a recovery until day 7. WS-1 was not detected in the leaves of either genotype. Withanone (WS-2) content in the leaves also decreased towards the end of the cold period in both genotypes. Cold stress also elicited the accumulation of WS-2 in AGB025, but was not detectable in control seedlings. At maturity, WS-2 was also detected in control plants. Furthermore, a significant increase in the leaf withaferin A (WS-3) content was recorded from day 1 to day 7 of the cold exposure in both the genotypes, suggesting the possible involvement of with-anolides in cold-protection. AGB002 showed comparatively higher accumulation of antioxidant enzymes and selected marker withanolides than AGB025, indicating that AGB002 is better adapted to cold than AGB025. It could be inferred from these observations that cold stress induces bioactive withanolide accu-mulation in W. somnifera as a mechanism for scavenging reactive oxygen species (ROS). These studies also provide an impetus for enhancing the withanolide accumulation in W. somnifera using controlled environment technology.

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“…Catalatic activity of the enzyme was monitored spectrophotometrically [27] by recording the decline of absorbance at 240 nm due to decomposition of H 2 O 2 (€= 40 M -1 cm -1 ). For in-gel activity assay, the crude protein extract was first separated in 10% native PAGE at 4℃ under constant current of 30 mA and the catalase activity in the gel was visualized through enzyme specific staining [28]. The protein concentration was measured following Bradford [29].…”

Section: Spectrophotometric and In-gel Assay Of Catalase Activitymentioning

confidence: 99%

Osmolyte modulated enhanced rice leaf catalase activity under salt-stress

Sahu¹,

Das²,

Ray³

et al. 2010

ABB

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Change in catalase activity was examined in leaves of rice plant exposed to salinity. Depending on the method of preparation of crude protein extract from leaf and the constituents of the assay medium, a significant difference in enzyme activity was recorded. Inclusion of sorbitol or mannitol or sucrose in the extraction and enzyme assay medium enhanced the enzyme activity in salt-stressed samples by nearly 1.5-1.8 fold, compared to the activity found in unstressed plants, which otherwise showed a 50% declined activity in leaf extract prepared in buffer solution and assayed in a medium depleted of these sugars. In view of the accumulation of osmolytes under saline condition, these observations suggest that the catalase activity is modulated by the osmolytes and maintains a high rate of hydrogen peroxide scavenging property in vivo and serves as the major antioxidant enzyme to scavenge the salt-induced formation of peroxide. Therefore, the salt-stress induced appearance of low activity of the enzyme under normal buffer extraction and assay conditions, as reported in literature may represent an apparent than for its real in vivo activity.

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An improved procedure using ferricyanide for detecting catalase isozymes

Cited by 625 publications

References 5 publications

Alterations in biochemical components in mesta plants infected with yellow vein mosaic disease

Alterations in biochemical components in mesta plants infected with yellow vein mosaic disease

Cold stress affects antioxidative response and accumulation of medicinally important withanolides in Withania somnifera (L.) Dunal

Osmolyte modulated enhanced rice leaf catalase activity under salt-stress

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