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. 1979 Aug;64(2):187–192. doi: 10.1104/pp.64.2.187

Subcellular Localization of the Starch Degradative and Biosynthetic Enzymes of Spinach Leaves 1

Thomas W Okita a, Elaine Greenberg a, David N Kuhn a,2, Jack Preiss a
PMCID: PMC543051  PMID: 16660929

Abstract

The subcellular localization of the starch biosynthetic and degradative enzymes of spinach leaves was carried out by measuring the distribution of the enzymes in a crude chloroplast pellet and soluble protein fraction, and by the separation on sucrose density gradients of intact organelles, chloroplasts, peroxisomes, and mitochondria of a protoplast lysate. ADP-Glucose pyrophosphorylase, starch synthase, and starch-branching enzymes are quantitatively associated with the chloroplasts. The starch degradative enzymes amylase, R-enzyme (debranching activity), phosphorylase, and D-enzyme (transglycosylase) are observed both in the chloroplast and soluble protein fractions, the bulk of the degradative enzyme activities reside in the latter fraction. Chromatography of a chloroplast extract on diethylaminoethyl-cellulose resolves the R- and D-enzymes from amylase and phosphorylase activities although the two latter enzyme activities coeluted. The digestion pattern of amylase with amylopectin as a substrate indicates an endolytic activity but displays properties unlike the typical α-amylase as isolated from endosperm tissue.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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