maltotriose/spinacia oleracea

The distribution of (14)C in the various glucose residues of maltotriose was studied as a function of time of photosynthesis of isolated chloroplasts of spinach (Spinacia oleracea L.) using (14)CO(2). The distribution of label showed that the reducing-end glucose residue was labeled first and the

Two major alpha-glucan phosphorylases (I and II) from leaves of the C(4) plant corn (Zea mays L.) were previously shown to be compartmented in mesophyll and bundle sheath cells, respectively (C Mateyka, C Schnarrenberger 1984 Plant Sci Lett 36: 119-123). The two enzymes were separated by

A glucosyl and a glucosyl-glucan transferase activity from spinach (Spinacia oleracea L. var. Matador) leaves have been partially purified and characterized. The latter activity (fraction 1 after diethylaminoethylcellulose chromatography) is responsible for the transfer of glucosyl as well as of

Transglucosylation activities of spinach alpha-glucosidase I and IV, which have different substrate specificity for hydrolyzing activity, were investigated. In a maltose mixture, alpha-glucosidase I, which has high activity toward not only maltooligosaccharides but also soluble starch and can

Multiple forms of ADP-glucose-alpha-1,4-glucan alpha-4-glucosyltransferase were obtained from spinach leaves by gradient elution from a DEAE-cellulose column. In the presence of high concentrations of some salts and bovine serum albumin, unprimed activity was found in one (transglucosylase III) of

The properties of two amylase activities which differ in their substrate specificity and subcellular location as well as a chloroplast-associated R-enzyme (debranching activity) are reported. An extrachloroplastic amylase is resolved by gel filtration chromatography into two activities of 80,000 and

Permeation of [14 C]maltose into the stroma (measured as the sorbitol-impermeable space) of isolated intact spinach (Spinacia oleracea L.) chloroplasts was studied using the silicone oil centrifugation technique. Maltose uptake showed Michaelis Menten-kinetics with a K(m) of 25 mM and a Vmax of 19.5