Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone

ISSN:
0031-9422
Keywords:
Petunia hybrida ; Solanaceae ; chalcone isomerase ; chalcone synthase. ; flavonoid pathway ; flower petals
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Type of Medium:
Electronic Resource
URL:
_version_ 1798291203816423424
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
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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