Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone
ISSN: |
0031-9422
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Keywords: |
Petunia hybrida ; Solanaceae ; chalcone isomerase ; chalcone synthase. ; flavonoid pathway ; flower petals
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798291203816423424 |
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autor | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
autorsonst | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
book_url | http://linkinghub.elsevier.com/retrieve/pii/S0031-9422(00)83023-X |
datenlieferant | nat_lic_papers |
fussnote | The isomerisation of 2',4,4',6'-tetrahydroxychalcone by the enzyme chalcone isomerase is difficult to assay accurately in view of the spontaneous cyclisation of this chalcone at the alkaline pH optimum of the enzyme. We report here that self-cyclisation of naringenin chalcone is dramatically reduced at pH-values =〈 6.5 and in the presence of high concentrations of serum albumin (5-10 mg ml ^-^1). We have critically evaluated existing assay procedures of chalcone isomerase, utilizing the effects of a monospecific anti-(chalcone isomerase) serum to distinguish between spontaneous and enzymic cyclisation of chalcone. We conclude that the modifications listed above considerably facilitate the measurement of chalcone isomerase kinetics. |
hauptsatz | hsatz_simple |
identnr | NLZ17553537X |
issn | 0031-9422 |
journal_name | Phytochemistry |
materialart | 1 |
package_name | Elsevier |
publikationsort | Amsterdam |
publisher | Elsevier |
reference | 24 (1985), S. 2267-2269 |
schlagwort | Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals |
search_space | articles |
shingle_author_1 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
shingle_author_2 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
shingle_author_3 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
shingle_author_4 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. |
shingle_catch_all_1 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals 0031-9422 00319422 Elsevier |
shingle_catch_all_2 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals 0031-9422 00319422 Elsevier |
shingle_catch_all_3 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals 0031-9422 00319422 Elsevier |
shingle_catch_all_4 | N.M. Mol, J. P. Robbinst, M. A. Dixon, R. Veltkamp, E. Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals Petunia hybrida Solanaceae chalcone isomerase chalcone synthase. flavonoid pathway flower petals 0031-9422 00319422 Elsevier |
shingle_title_1 | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone |
shingle_title_2 | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone |
shingle_title_3 | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone |
shingle_title_4 | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone |
sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
timestamp | 2024-05-06T08:28:53.591Z |
titel | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone |
titel_suche | Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone The isomerisation of 2',4,4',6'-tetrahydroxychalcone by the enzyme chalcone isomerase is difficult to assay accurately in view of the spontaneous cyclisation of this chalcone at the alkaline pH optimum of the enzyme. We report here that self-cyclisation of naringenin chalcone is dramatically reduced at pH-values =〈 6.5 and in the presence of high concentrations of serum albumin (5-10 mg ml ^-^1). We have critically evaluated existing assay procedures of chalcone isomerase, utilizing the effects of a monospecific anti-(chalcone isomerase) serum to distinguish between spontaneous and enzymic cyclisation of chalcone. We conclude that the modifications listed above considerably facilitate the measurement of chalcone isomerase kinetics. |
topic | W V |
uid | nat_lic_papers_NLZ17553537X |