Differentiation of the Properties of the Branching Isozymes from Maize (Zea mays)
Year: 1993
Type: article
Abstract: The multiple forms of branching enzyme (BE) from developing maize (Zea mays) endosperm were purified by modification of previous procedures such that amylase activity could be eliminated completely from the BE preparation. Three distinct assays for BE activity (phosphorylase a stimulation assay, BE linkage assay, and iodine stain assay) were used to characterize and differentiate the properties of the BE isoforms. This study presents the first evidence that the BE isoforms differ in their action on amylopectin. BEI had the highest activity in branching amylose, but its rate of branching amylopectin was less than 5% of that of branching amylose. Conversely, BEII isoforms had lower rates in branching amylose (about 9-12% of that of BEI) and had higher rates of branching amylopectin (about 6-fold) than BEI. The implication of these findings to the mechanism of amylopectin synthesis in vivo are discussed.
Source: PLANT PHYSIOLOGY
Authors: H. P. Guan, J. Preiss
Institution: Michigan State University
Language: English
Subfield: Biochemistry
Domain: Life Sciences
SDG: Zero hunger
Open Access status: green
Funder: U.S. Department of Agriculture
OpenAlex ID: W2133361436
