Claim · model-written summary
An increase in extinction coefficient and lambda(max) is detected when debranched amylopectin and beta-limit amylopectin form a complex with I2-KI in spinach.
- Taxon
- Spinach
Spinacia oleraceat0 - Compound
- I(2)-KIe3
- Outcome
- extinction coefficient and lambda(max)e3
- Direction
- increasee3
Not reportedMaterialGeneOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Verbatim
t0“Starch Degradation in Spinach Leaves”
e3“An increase in extinction coefficient and lambda(max) is detected when the debranched amylopectin and beta-limit amylopectin form a complex with I(2)-KI”
Title
Starch Degradation in Spinach Leaves
Thomas W. Okita; Jack Preiss PLANT PHYSIOLOGY 1980. doi:10.1104/pp.66.5.870
Other claims from this paper (17)
- Observation Extrachloroplastic amylase activity resolves by gel filtration into two activities of 80,000 and 40,000 daltons in spinach leaves.
- Observation Both extrachloroplastic amylase activities hydrolyze amylopectin and shellfish glycogen in spinach leaves.
- Observation Both extrachloroplastic amylase activities hydrolyze rabbit liver glycogen, beta-limit amylopectin and amylose only slowly in spinach leaves.
- Observation The major chloroplastic amylase of spinach leaves attacks all tested glucans at comparable rates.
- Observation Glucan hydrolysis by both spinach leaf amylases generates appreciable amounts of oligosaccharides besides maltose.
- Observation Maltotetraose hydrolysis by spinach leaf amylases produces glucose, maltose and maltotriose.
- Observation The action patterns indicate that both spinach leaf amylase activities are endoamylases.
- Observation Spinach leaf amylases lack the typical Ca(2+) requirement or heat stability of seed endosperm alpha-amylases.
- Intervention effect Dithiothreitol had no effect on chloroplastic or extrachloroplastic amylase activities of spinach leaves.
- Intervention effect Glutathione (oxidized or reduced) had no effect on chloroplastic or extrachloroplastic amylase activities of spinach leaves.
- Intervention effect Ascorbate had no effect on chloroplastic or extrachloroplastic amylase activities of spinach leaves.
- Intervention effect Dehydroascorbate had no effect on chloroplastic or extrachloroplastic amylase activities of spinach leaves.
- Intervention effect Dithiothreitol plus thioredoxin had no effect on chloroplastic or extrachloroplastic amylase activities of spinach leaves.
- Observation The chloroplastic R-enzyme of spinach leaves debranches amylopectin, beta-limit amylopectin and pullulan.
- Observation The chloroplastic R-enzyme of spinach leaves debranches alpha-limit dextrins.
- Observation The chloroplastic R-enzyme of spinach leaves does not debranch rabbit liver glycogen.
- Association The chloroplastic R-enzyme of spinach leaves is similar in enzymic activity to the R-enzyme of endosperm tissue.