1993
DOI: 10.1104/pp.101.1.73
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Starch Degradation and Distribution of the Starch-Degrading Enzymes in Vicia faba Leaves (Diurnal Oscillation of Amylolytic Activity and Starch Content in Chloroplasts)

Abstract: ~~ ~Subcellular localization of the starch-degrading enzymes in Vicia faba leaves was achieved by an electrophoretic transfer method through a starch-containing gel (SCC) and enzyme activity measurements. Total amylolytic and phosphorolytic activities were found predominantly in the extrachloroplastic fraction, whereas the debranching enzymes showed homogenous distribution between stromal and extrachloroplastic fractions. Staining of end products in the SCC revealed two isoforms of a-amylase (EC

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Cited by 28 publications
(5 citation statements)
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“…As a result, the higher starch values obtained by the perchloric acid method can be related to the greater acid strength of HClO 4 compared to that of HCl. In this sense, perchloric acid has been considered to be the most efficient solvent for starch extraction from plant tissues (Ghiena et al 1993).…”
Section: Resultsmentioning
confidence: 99%
“…As a result, the higher starch values obtained by the perchloric acid method can be related to the greater acid strength of HClO 4 compared to that of HCl. In this sense, perchloric acid has been considered to be the most efficient solvent for starch extraction from plant tissues (Ghiena et al 1993).…”
Section: Resultsmentioning
confidence: 99%
“…BAMs are known to play an important role in chloroplast starch degradation, but little is known about the properties of these enzymes, in part because there are multiple isozymes but more importantly, because of the masking of their activity by a potentially abundant extrachloroplastic BAM (Caspar et al, 1989;Ghiena et al, 1993). Genetic evidence was used to show that BAM3 is the primary enzyme acting on starch at night, because mutants lacking or with diminished BAM3 have a starch-excess phenotype (Kaplan and Guy, 2005;Fulton et al, 2008).…”
Section: Discussionmentioning
confidence: 99%
“…Β-amylases catalyze the hydrolysis of a-1, 4-glycosidic linkages and release maltose from the exposed nonreducing ends of glucan chains. Α-amylases hydrolyze α-1, 4 linkages within polymers exposed on the surface or in channels within granules, releasing soluble glucans that are the substrate for further degradation [ 60 , 61 ]. In this study, there no significant changes were observed for the expression of transcript-encoding GWD.…”
Section: Discussionmentioning
confidence: 99%