Phytoalexin production in French bean leaves infected by botrytis cinerea

1978 ◽  
Vol 84 (2) ◽  
pp. 37-46 ◽  
Author(s):  
J. Heuvel ◽  
Dineke Grootveld
Keyword(s):  
Botrytis Cinerea ◽  
French Bean ◽  
Bean Leaves

Purification and characterization of a constitutive polygalacturonase associated with the infection process of French bean leaves by Botrytis cinerea

1990 ◽  
Vol 68 (9) ◽  
pp. 1921-1930 ◽  
Author(s):  
G. Leone ◽  
E. A. M. Schoffelmeer ◽  
J. Van den Heuvel
Keyword(s):  
Botrytis Cinerea ◽  
Reaction Rate ◽  
French Bean ◽  
Infection Process ◽  
Purification Procedure ◽  
Purification And Characterization ◽  
Titration Curves ◽  
Optimal Ph ◽  
Bean Leaves

The constitutively produced polygalacturonase isoenzyme PG2 was isolated from culture filtrates of Botrytis cinerea, purified to homogeneity, and characterized. The shape of titration curves of PG2 and two other polygalacturonase isoenzymes explained the difficulties found in separating superimposed pectic enzyme activities during the purification procedure. PG2 hydrolyzed sodium polygalacturonate more quickly than pectin. The optimal pH for PG2 activity with polygalacturonate was 4.5 and with pectin, 4.0. PG2 activity was also influenced by the presence of NaCl or CaCl2 in the reaction mixture. Analysis of the breakdown products by paper chromatography and a comparison of the reaction rate by viscosimetry and reducing group assay revealed that PG2 has an endocatalytic mode of action on polygalacturonate. The isoelectric point and the molecular mass of PG2 were estimated to be 9.1 and 23.0 kDa, respectively. Key words: Botrytis cinerea, chromatofocusing, endopolygalacturonase, purification, substrate specificity, titration curve.

scholarly journals Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase

1972 ◽  
Vol 128 (2) ◽  
pp. 229-235 ◽  
Author(s):  
D. C. Shaw ◽  
J. R. E. Wells
Keyword(s):  
Amino Acids ◽  
French Bean ◽  
Unique Sequence ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Serine Carboxypeptidase ◽  
Serine Residue ◽  
Radiochemical Determination ◽  
Bean Leaves

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [32P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ‘serine’ enzymes previously reported and, for phaseolain, represents an unequivocal example of a ‘serine’ carboxypeptidase.

A method for 13 C-labeling of metabolic carbohydrates within French bean leaves (Phaseolus vulgaris L.) for decomposition studies in soils

2009 ◽  
Vol 23 (12) ◽  
pp. 1792-1800 ◽  
Author(s):  
Cyril Girardin ◽  
Daniel P. Rasse ◽  
Philippe Biron ◽  
Jaleh Ghashghaie ◽  
Claire Chenu
Keyword(s):  
Phaseolus Vulgaris ◽  
French Bean ◽  
Phaseolus Vulgaris L ◽  
Bean Leaves
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