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Related Experiment Video

Updated: Jun 25, 2026

Purification of Mitochondria from Yeast Cells

Purification of Mitochondria from Yeast Cells

Published on: August 24, 2009

Purification and properties of sucrose synthase from maize kernels.

J C Su¹, J Preiss

¹Department of Biochemistry and Biophysics, University of California, Davis, California 95616.

Plant Physiology

|March 1, 1978

Summary

This summary is machine-generated.

Maize sucrose synthase was purified, revealing identical subunits that form various active aggregates. The tetrameric form is predominant and exhibits the highest specific activity, suggesting it is the native enzyme structure.

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Published on: February 15, 2019

Area of Science:

Biochemistry
Plant Science
Enzymology

Background:

Sucrose synthase is a key enzyme in carbohydrate metabolism in plants.
Understanding its structure and activity is crucial for maize kernel development.

Purpose of the Study:

To purify and characterize sucrose synthase from maize kernels.
To investigate the enzyme's subunit composition and aggregation states.
To determine the native and most active form of the enzyme.

Main Methods:

Purification using ammonium sulfate fractionation, gel filtration (Sephadex G-200), and affinity chromatography (UDP-hexanol-amino-agarose).
Analysis of enzyme forms using polyacrylamide gel electrophoresis, sedimentation velocity, and gel filtration.
Determination of molecular weight and N-terminal status.

Main Results:

Sucrose synthase was purified 42-fold with over 80% yield.
The enzyme consists of identical subunits and forms tetrameric, octameric, and higher aggregates.
All forms are catalytically active, with the tetramer being predominant and having the highest specific activity.
The subunit molecular weight is 88,000, and the N-terminus is blocked.

Conclusions:

The tetrameric form of sucrose synthase is likely the native and most active conformation in maize kernels.
The enzyme's aggregation state influences its specific activity.
The blocked N-terminus may have implications for enzyme regulation or stability.