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. 1972 Feb;126(4):953–963. doi: 10.1042/bj1260953

Soluble adenosine diphosphate glucose–α-1,4-glucan α-4-glucosyltransferases from spinach leaves

J L Ozbun 1,*, J S Hawker 1,†, Jack Preiss 1
PMCID: PMC1178503  PMID: 5073245

Abstract

Multiple forms of ADP-glucose–α-1,4-glucan α-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 four fractions eluted from the column. In addition to having unprimed activity, transglucosylase III had a lower Km for ADP-glucose, a much higher Km for oyster glycogen, greater heat sensitivity and lower affinity for maltose, maltotriose and amylopectin β-limit dextrin than fractions I, II and IV. In addition, the kinetics at low concentrations of amylose, amylopectin and rabbit liver glycogen were non-linear for transglucosylase III. The properties of transglucosylases I, II and IV were generally similar to each other. Rates of the unprimed reaction at physiological concentrations of ADP-glucose were greater than those found for the primed reaction of fraction III. The product formed by the unprimed reaction was a glucan containing principally α-1,4 linkages with some α-1,6 linkages. The primer, maltose, at a concentration of 0.5m inhibited the synthesis of the unprimed product.

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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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