Upper limits for endogenous oligogalacturonides and free galacturonic acid in rose cell-suspension cultures: Implications for the action of Exo- and Endo-polygalacturonases in vivo

1997 ◽  
Vol 150 (3) ◽  
pp. 241-246 ◽  
Author(s):  
Inmaculada García-Romera ◽  
Stephen C. Fry
1972 ◽  
Vol 27 (8) ◽  
pp. 946-954 ◽  
Author(s):  
Wolfgang Hösel ◽  
Paul D. Shaw ◽  
Wolfgang Barz

The flavonols kaempferol, quercetin and isorhamnetin were labelled with 14C by keeping seven day old Cicer arietinum L. plants in an atmosphere of 14CO2 for five days. The purified (U-14C) flavonols were applied to cell suspension cultures of Cicer arietinum L., Phaseolus aureus Roxb., Glycine max and Petroselinum hortense. Based on the rates of 14CO2 formation and distribution of radioactivity after fractionation of the cells, the flavonols were shown to be catabolized to a very high extent.All four cell suspension cultures possess the enzymatic activity transforming flavonols to the recently discovered 2,3-dihydroxyflavanones. Upon incubation of the flavonols datiscetin and kaempferol with enzyme preparations from Cicer arietinum L. cell suspension cultures, it was demonstrated that the enzymatically formed 2,3-dihydroxyflavanones are further transformed in an enzyme catalyzed reaction. Salicylic acid was found as a degradation fragment of ring B of the 2,3,5,7,2′-pentahydroxyflavanone derived from datiscetin. Neither phloroglucinol nor phloroglucinol carboxylic acid were observed as metabolites of ring A. These in vitro findings were further substantiated by in vivo data because the flavonols kaempferol, quercetin and datiscetin when applied to cell suspension cultures of Cicer arietinum L. and Glycine max gave rise to para-hydroxybenzoic acid, protocatechuic acid and salicylic acid, respectively. It was thus concluded that flavonols are catabolized via 2,3-dihydroxyflavanones with the B-ring liberated as the respective benzoic acid. The data are discussed in connection with earlier findings on the catabolism of chalcones, cinnamic and benzoic acids.


1975 ◽  
Vol 30 (9-10) ◽  
pp. 650-658 ◽  
Author(s):  
Jochen Berlin ◽  
Wolfgang Barz

Oxidative decarboxylation of p-hydroxybenzoic acids in plant cell suspension cultures is catalyzed by peroxidases. This reaction has been characterized in vivo and in vitro. Decarboxylation of substituted benzoic acids yields monomeric, dimeric and oligomeric benzoquinones. All peroxidases obtained from soybean (Glycine max) cell suspension cultures by gel electrophoresis are equally capable to decarboxylate p-hydroxybenzoic acids as indicated by their rather low differences in specific activity for various benzoic acids.


Weed Science ◽  
1994 ◽  
Vol 42 (4) ◽  
pp. 509-516 ◽  
Author(s):  
Jon E. Scott ◽  
Leslie A. Weston ◽  
Joseph Chappell ◽  
Kathleen Hanley

Laboratory assays were conducted to determine the sensitivity of tomato and tobacco cell suspension cultures and tomato and pepper cotyledons to clomazone. A comparison of fresh weight and carotenoid content indicated up to a three-fold difference between the clomazone-tolerant tobacco and clomazone-susceptible tomato cell suspension cultures. In contrast, an approximate 60-fold difference between the tolerant pepper and susceptible tomato cotyledons was observed when total chlorophyll and carotenoid contents were measured. The effect of clomazone and its possible metabolites on in vivo and in vitro extractable IPP isomerase (EC 5.3.3.2) and prenyltransferase (EC 2.5.1.29) activity was investigated. There was no clear inhibitory effect of clomazone or possible clomazone metabolites upon enzyme activity in tomato or tobacco cell suspension cultures or on light or dark grown tomato or pepper cotyledons. No specific enzymatic target site of clomazone was identified in correlation with the reduction in total chlorophyll or carotenoid content.


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