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The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
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Journal Article
The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
1996
Overview
Preparations enriched in plastics were used to investigate the location of ADP-glucose pyrophosphorylase (AGPase) in the developing endosperm of maize (Zea mays L.). These preparations contained more than 25% of the total activity of the plastic marker enzymes alkaline pyrophosphatase and soluble starch synthase, less than 2% of the cytosolic marker enzymes alcohol dehydrogenase and pyrophosphate, fructose 6-phosphate 1-phosphotransferase, and approximately 3% of the AGPase activity. Comparison with the marker enzyme distribution suggests that more than 95% of the activity of AGPase in maize endosperm is extra-plastidial. Two proteins were recognized by antibodies to the small subunit of AGPase from maize endosperm Brittle-2 (Bt2). The larger of the two proteins was the major small subunit in homogenates of maize endosperm, and the smaller, less abundant of the two proteins was enriched in preparations containing plastics. These results suggest that there are distinct plastidial and cytosolic forms of AGPase, which are composed of different subunits. Consistent with this was the finding that the bt2 mutation specifically eliminated the extra-plastidial AGPase activity and the larger of the two proteins recognized by the antibody to the Bt2 subunit
Publisher
American Society of Plant Physiologists
Subject
/ Alcohol Dehydrogenase - analysis
/ analysis
/ Biological and medical sciences
/ Corn
/ Cytosol
/ Embryos
/ Enzymes
/ Fundamental and applied biological sciences. Psychology
/ genetics
/ Glucose-1-Phosphate Adenylyltransferase
/ Nucleotidyltransferases - analysis
/ Nucleotidyltransferases - genetics
/ Peas
/ Plant physiology and development
/ Plants
/ PLASTE
/ Plastids
/ Seeds
/ Starch
/ Starches
/ Subcellular Fractions - enzymology
/ Sucrose
/ ZEA MAYS
