Growth and cell wall composition of glucose-limited bean cells (Phaseolus vulgaris L.)

1982 ◽  
Vol 1 (3) ◽  
pp. 131-134
Author(s):  
M. A. Bertola ◽  
R. G. M. Roemer ◽  
F. M. Klis
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Cell Wall Composition ◽  
Phaseolus Vulgaris L

scholarly journals Cell-Wall Proteins Induced by Water Deficit in Bean (Phaseolus vulgaris L.) Seedlings

1995 ◽  
Vol 107 (4) ◽  
pp. 1119-1128 ◽  
Author(s):  
A. A. Covarrubias ◽  
J. W. Ayala ◽  
J. L. Reyes ◽  
M. Hernandez ◽  
A. Garciarrubio
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Water Deficit ◽  
Cell Wall Proteins ◽  
Phaseolus Vulgaris L

scholarly journals Cell wall polysaccharide biosynthesis and related metabolism in elicitor-stressed cells of French bean (Phaseolus vulgaris L.)

1995 ◽  
Vol 306 (3) ◽  
pp. 745-750 ◽  
Author(s):  
D Robertson ◽  
B A McCormack ◽  
G P Bolwell
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Time Course ◽  
Glucose Dehydrogenase ◽  
French Bean ◽  
Primary Cell Wall ◽  
Cell Wall Polysaccharide ◽  
Phaseolus Vulgaris L ◽  
Glucan Synthase ◽  
Elicitor Treatment

Enzyme activities involved in quantitative and qualitative flux of sugars into cell wall polysaccharides were determined following elicitor treatment of suspension cultured cells of French bean (Phaseolus vulgaris L.). Two subsets of activities were examined: the first were involved in synthesis and metabolism of UDP-glucose and the provision of the pool of UDP-sugars, and the second a selection of membrane-bound glycosyltransferases involved in the synthesis of pectins, hemicelluloses and glucans of the primary cell wall. Of the first group, only UDP-glucose dehydrogenase (EC 1.1.1.22) showed any significant induction in response to elicitor treatment, sucrose synthase (EC 2.4.1.13), UDP-glucuronate decarboxylase (EC 4.1.1.35), UDP-glucose and UDP-xylose 4-epimerases (EC 5.1.3.2 and EC 5.1.3.5 respectively) did not change in activity significantly over the time course. In contrast, enzymes of the second group showed a more complex response. Callose synthase (glucan synthase II, EC 2.4.1.12) increased in activity, as has been shown in other systems, while arabinan synthase (EC 2.4.1.-), xylan synthase (EC 2.4.1.72), xyloglucan synthase (EC 2.4.1.72) and glucan synthase I (EC 2.4.1.12) activities were rapidly depleted from membranes within 3 h following elicitor action. This rapid turnover of activity was striking, indicating that the half-life of such enzymes can be short and that elicitor action causes substantial perturbation of some membrane activities. Glucan synthase I activity appears to increase in the later stages over the time period measured, indicating some recovery of this metabolism.

Cell Wall Dissolution during Industrial Processing of Green Beans (Phaseolus vulgaris L.)

1995 ◽  
Vol 43 (9) ◽  
pp. 2480-2486 ◽  
Author(s):  
Trinette Stolle-Smits ◽  
Jan G. Beekhuizen ◽  
Cees van Dijk ◽  
Alfons G. J. Voragen ◽  
Kees Recourt
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Phaseolus Vulgaris L ◽  
Green Beans ◽  
Industrial Processing

FTIR spectroscopy monitoring of cell wall modifications during the habituation of bean (Phaseolus vulgaris L.) callus cultures to dichlobenil

Plant Science ◽  
2004 ◽  
Vol 167 (6) ◽  
pp. 1273-1281 ◽  
Author(s):  
Ana Alonso-Simón ◽  
Antonio E. Encina ◽  
Penélope García-Angulo ◽  
Jesús M. Álvarez ◽  
José L. Acebes
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Ftir Spectroscopy ◽  
Callus Cultures ◽  
Phaseolus Vulgaris L

scholarly journals Synthesis of dehydrogenation polymers of ferulic acid with high specificity by a purified cell-wall peroxidase from French bean (Phaseolus vulgaris L.)

1994 ◽  
Vol 299 (3) ◽  
pp. 747-753 ◽  
Author(s):  
A Zimmerlin ◽  
P Wojtaszek ◽  
G P Bolwell
Keyword(s):  
Cell Wall ◽  
Phaseolus Vulgaris ◽  
Ferulic Acid ◽  
Cultured Cells ◽  
Gel Filtration ◽  
High Specificity ◽  
French Bean ◽  
Good Evidence ◽  
Ionization Mass ◽  
Phaseolus Vulgaris L

A cationic (pI 8.3) wall-bound peroxidase has been purified to homogeneity from suspension-cultured cells of French bean (Phaseolus vulgaris L.). The enzyme was a glycoprotein and its M(r) was 46,000 as determined by SDS/Page and h.p.l.c. gel filtration. It was localized biochemically to microsomes and the cell wall, and the latter subcellular distribution was confirmed by immunogold techniques. The native enzyme showed absorption maxima at 403, 500 and 640 nm, with an RZ (A405/A280) of 3.3. The peroxidase oxidized guaïacol and natural phenolic acids. By desorption-chemical-ionization mass spectrometry the enzyme was found to oxidize the model compound, ferulic acid, into dehydrodiferulic acid. Kinetics studies indicated an apparent Km of 113.3 +/- 22.9 microM and a Vmax of 144 mumol.min-1.nmol-1 of protein at an H2O2 concentration of 100 microM. In comparison with a second French-bean peroxidase (FBP) and horseradish peroxidase, as a model, it acted with a 6-10-fold higher specificity in this capacity. It is a member of the peroxidase superfamily of bacterial, fungal and plant haem proteins by virtue of its highly conserved amino acid sequence within the proximal and distal haem-binding sites. This is good evidence that this particular FBP may function in constructing covalent cross-linkages in the wall during development and response to pathogens.

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