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Subunit Structure of Spinach Leaf ADPglucose Pyrophosphorylase

Open access
Morell, Matthew K., Bloom, Mark, Knowles, Vicki, Preiss, Jack·1987·Plant Physiology

Abstract

To initiate structural studies of the ADPglucose pyrophosphorylase from spinach an improved purification procedure was devised. The modified purification scheme allowed the isolation of 20 to 30 milligrams pure enzyme from 10 kilogram of spinach leaves. Electrophoresis of the purified enzyme confirmed an earlier study which showed that the enzyme was putatively composed of two subunits (Copeland L, J Preiss 1981 Plant Physiol 68: 996-1001). The two subunits migrate as 51 and 54 kilodalton proteins upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both proteins can be detected on Western blots of leaf homogenates prepared under denaturing conditions suggesting that both subunits exist in vivo. Anion-exchange chromatography in the presence of urea allowed resolution of the 51 and 54 kilodalton proteins. They possess different N-terminal amino acid sequences and tryptic peptide maps. Western blot analysis reveals that the 51 and 54 kilodalton proteins are antigenically dissimilar. The 51 but not the 54 kilodalton protein is immunologically related to the ADPglucose pyrophosphorylase from maize endosperm and potato tuber.

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Metadata

Authors
Morell, M. K., Bloom, M., Knowles, V., & Preiss, J.
Venue
Plant Physiology
Published
1987-09-01
Volume
85
Issue
1
Pages
182-187
ISSN
  • 0032-0889 (ISSN-L)
  • 1532-2548
OpenAlex
W2014890562
Cited by
164
References
0
FWCI
4.05
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Subunit Structure of Spinach Leaf ADPglucose Pyrophosphorylase. https://app.cochat.ai/papers/10.1104/pp.85.1.182
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Morell, M. K., Bloom, M., Knowles, V., & Preiss, J. (1987). Subunit Structure of Spinach Leaf ADPglucose Pyrophosphorylase. Plant Physiology. https://doi.org/10.1104/pp.85.1.182

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