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Differentiation of the Properties of the Branching Isozymes from Maize (Zea mays)

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Guan, H. P., Preiss, J.·1993·Plant Physiology

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.

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Metadata

Authors
Guan, H. P., & Preiss, J.
Venue
Plant Physiology
Published
1993-08-01
Volume
102
Issue
4
Pages
1269-1273
ISSN
  • 0032-0889 (ISSN-L)
  • 1532-2548
OpenAlex
W2133361436
Cited by
256
References
1
FWCI
6.90
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Differentiation of the Properties of the Branching Isozymes from Maize (Zea mays). https://app.cochat.ai/papers/10.1104/pp.102.4.1269
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Guan, H. P., & Preiss, J. (1993). Differentiation of the Properties of the Branching Isozymes from Maize (Zea mays). Plant Physiology. https://doi.org/10.1104/pp.102.4.1269

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