Localization of alpha-amylase in the apoplast of pea (Pisum sativum L.) stems

Most of the activity of an α-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 α-amylase is present in pea stems, representing approximately 6% of total stem amylolytic activ...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1988-08, Vol.87 (4), p.799-802
Main Authors: Beers, E.P, Duke, S.H
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
AMILASAS
AMYLASE
AMYLASES
Barley
Biological and medical sciences
Cell biochemistry
Cell physiology
Chloroplasts
Communications
Enzymes
ENZYMIC ACTIVITY
Fundamental and applied biological sciences. Psychology
Gels
Leaves
Metabolism and Enzymology
Peas
PISUM SATIVUM
Plant physiology and development
Plants
PLASTE
PLASTIDIOS
PLASTIDS
Protoplasts
Starches
STEMS
TALLO
TIGE
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Summary:Most of the activity of an α-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 α-amylase is present in pea stems, representing approximately 6% of total stem amylolytic activity and virtually all of the α-amylase activity. By a simple infiltration-extraction procedure, the majority (87%) of this α-amylase activity was recovered from the pea stem apoplast without significantly disrupting the symplastic component of the tissue. Only 3% of the β-amylase activity and less than 2% of other cellular marker enzymes were removed during infiltration-extraction.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.87.4.799