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Beers EP, Duke SH. Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems. Plant Physiol. 1988;87(4):799-802doi: 10.1104/pp.87.4.799.
Beers, E. P., & Duke, S. H. (1988). Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems. Plant physiology, 87(4), 799-802. https://doi.org/10.1104/pp.87.4.799
Beers, E P, and Duke, S H. "Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems." Plant physiology vol. 87,4 (1988): 799-802. doi: https://doi.org/10.1104/pp.87.4.799
Beers EP, Duke SH. Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems. Plant Physiol. 1988 Aug;87(4):799-802. doi: 10.1104/pp.87.4.799. PMID: 16666227; PMCID: PMC1054847.
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Plant Physiol. 1988 Aug;87(4):799-802. doi: 10.1104/pp.87.4.799.

Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems.

Plant physiology

E P Beers, S H Duke

Affiliations

  1. Department of Agronomy, University of Wisconsin, Madison, Wisconsin 53706.

PMID: 16666227 PMCID: PMC1054847 DOI: 10.1104/pp.87.4.799

Abstract

Most of the activity of an alpha-amylase present in crude pea (Pisum sativum L. cv Laxton's Progress No. 9) leaf preparations cannot be found in isolated pea leaf protoplasts. The same extrachloroplastic alpha-amylase is present in pea stems, representing approximately 6% of total stem amylolytic activity and virtually all of the alpha-amylase activity. By a simple infiltration-extraction procedure, the majority (87%) of this alpha-amylase activity was recovered from the pea stem apoplast without significantly disrupting the symplastic component of the tissue. Only 3% of the beta-amylase activity and less than 2% of other cellular marker enzymes were removed during infiltration-extraction.

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