Purification and characterization of flavone-specific ?-glucuronidase from callus cultures of Scutellaria baicalensis Georgi

Morimoto, Satoshi; Harioka, T.; Shoyama, Yukihiro

doi:10.1007/bf00195712

Cited by 33 publications

(33 citation statements)

References 16 publications

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“…It indicates that the baicalin-b-D-glucuronidase is a flavone-specific bglucuronidase, which has higher activity of hydrolyzing baicalin (baicalein 7-O-b-D-glucuronide) than that of pnitrophenyl-b-D-glucuronide and p-phenolphthalein-b-Dglucuronide (Table 3). This result is the same as that of Morimoto [15], and similar to our previous study in ginsenoside-b-glucosidase and glucosidase [16].…”

Section: Substrate Specificity Of Baicalin-b-d-glucuronidasesupporting

confidence: 81%

Purification and characterization of baicalin-β-d-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge

Zhang

Chen

et al. 2005

Process Biochemistry

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Section: Substrate Specificity Of Baicalin-b-d-glucuronidasesupporting

confidence: 81%

Purification and characterization of baicalin-β-d-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge

Zhang

Chen

et al. 2005

Process Biochemistry

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“…Stress Treatment of Scutellaria Calluses-The four-week-old calluses of Scutellaria baicalensis (5 g), which was cultured on Murashige-Skoog medium (21) as described previously (20), were subdivided into 100-ml flasks, and 20 ml of liquid Murashige-Skoog medium was added to each flask. After 200 l of 10% (v/w) yeast extract dissolved in the liquid Murashige-Skoog medium was added (final concentration of yeast extract, 0.1%), the calluses were incubated at 25°C for 3 h. Treatment of the callus with H 2 O 2 was conducted as described above, except that 100 l of 1 M H 2 O 2 (final H 2 O 2 concentration, 5 mM) was used instead of the yeast extract solution.…”

Section: Methodsmentioning

confidence: 99%

Identification and Molecular Characterization of Novel Peroxidase with Structural Protein-like Properties

Morimoto

Tateishi

Inuyama

et al. 1999

Journal of Biological Chemistry

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Elicitor treatment or mechanical damage to Scutellaria baicalensis Georgi (skullcap plants) callus causes an immediate insolubilization of a 36-kDa protein into cell walls. The 36-kDa protein was identified as peroxidase 1 by analysis of its internal amino acid sequence and by immunoblotting using affinity-purified anti-peroxidase 1. Insolubilized peroxidase 1 is cross-linked to lignin through covalent bonds, and the cross-linking is catalyzed in the presence of H 2 O 2 by peroxidase 1 itself. The properties of insolubilized peroxidase 1 resemble those of defense-related structural proteins (extensins and proline-rich proteins) cross-linked to cell wall. Although the isozymes peroxidases 2 and 3 have enzyme activities similar to peroxidase 1, they are not insolubilized by stress treatment. Molecular characterization established that peroxidase 1 contains regions characteristic of structural proteins, but peroxidases 2 and 3 do not have such regions. These results suggest that among the three isozymes, only peroxidase 1 has a structural protein-like function as well as an enzymatic function.

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“…In addition, this plant has long been known to possess a ␤-glucuronidase, called baicalinase (16). Previously, we purified ␤-glucuronidase from the callus culture and demonstrated that this enzyme displays high activity for baicalein 7-O-␤-D-glucuronide (BAG), the main flavonoid of this plant (17). To establish the physiological roles of ␤-glucuronidase and BAG, we attempted further studies.…”

mentioning

confidence: 99%

Novel Hydrogen Peroxide Metabolism in Suspension Cells ofScutellaria baicalensis Georgi

Morimoto

Tateishi

Matsuda

et al. 1998

Journal of Biological Chemistry

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We identified a rapid and novel system to effectively metabolize a large amount of H 2 O 2 in the suspension cells of Scutellaria baicalensis Georgi. In response to an elicitor, the cells immediately initiate the hydrolysis of baicalein 7-O-␤-D-glucuronide by ␤-glucuronidase, and the released baicalein is then quickly oxidized to 6,7-dehydrobaicalein by peroxidases. Hydrogen peroxide is effectively consumed during the peroxidase reaction. The ␤-glucuronidase inhibitor, saccharic acid 1,4-lactone, significantly reduced the H 2 O 2 -metabolizing ability of the Scutellaria cells, indicating that ␤-glucuronidase, which does not catalyze the H 2 O 2 degradation, plays an important role in the H 2 O 2 metabolism. As H 2 O 2 -metabolizing enzymes, we purified two peroxidases using ammonium sulfate precipitation followed by sequential chromatography on CM-cellulose and hydroxylapatite. Both peroxidases show high H 2 O 2 -metabolizing activity using baicalein, whereas other endogenous flavones are not substrates of the peroxidase reaction. Therefore, baicalein predominantly contributed to H 2 O 2 metabolism. Because ␤-glucuronidase, cell wall peroxidases, and baicalein pre-exist in Scutellaria cells, their constitutive presence enables the cells to rapidly induce the H 2 O 2 -metabolizing system.

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Purification and characterization of flavone-specific ?-glucuronidase from callus cultures of Scutellaria baicalensis Georgi

Cited by 33 publications

References 16 publications

Purification and characterization of baicalin-β-d-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge

Purification and characterization of baicalin-β-d-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge

Identification and Molecular Characterization of Novel Peroxidase with Structural Protein-like Properties

Novel Hydrogen Peroxide Metabolism in Suspension Cells ofScutellaria baicalensis Georgi

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