alpha maltose/špinat

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Transglucosylation activities of multiple forms of alpha-glucosidase from spinach.

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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

Characterization of maltose biosynthesis from α-D-glucose-1-phosphate in Spinacia oleracea. L.

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The de novo synthesis of maltose in spinach (Spinacia oleracea L.) was shown to be catalyzed by a maltose synthase, which converts two molecules of α-D-glucose-1-phosphate (α-G1P) (Km 1.5 mmol l(-1)) to maltose and 2 orthophosphate (Pi). This enzyme was purified 203-fold by fractionated ammonium

Integration of the thylakoid membrane protein cytochrome b6 in the cytoplasmic membrane of Escherichia coli.

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An overexpression system for spinach apocytochrome b(6) as a fusion protein to a maltose-binding protein in Escherichia coli was established using the expression vector pMalp2. The fusion of the cytochrome b(6) to the periplasmic maltose-binding protein directs the cytochrome on the Sec-dependent

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