Purification and characterization of actin from maize pollen
1Laboratory of Plant Biochemistry, College of Biological Sciences, Beijing Agricultural University, Beijing 100094, China.
Plant Physiology
|July 1, 1992
Summary
Researchers purified plant actin from maize (Zea mays L.) pollen, finding it biochemically similar to muscle actin. This pollen actin effectively activates muscle myosin ATPase, highlighting its potential for actomyosin system studies.
Area of Science:
- Biochemistry
- Plant Physiology
- Molecular Biology
Background:
- Pollen is a valuable resource for studying the plant actomyosin system.
- Efficient actin purification methods are crucial for biochemical and physiological research.
Purpose of the Study:
- To develop an efficient method for purifying actin from maize (Zea mays L.) pollen.
- To characterize the biochemical properties of purified pollen actin.
- To assess the functional activity of pollen actin in the actomyosin system.
Main Methods:
- Acetone powder preparation
- Ammonium sulfate fractionation
- Ion-exchange chromatography (DEAE-cellulose)
- Polymerization-depolymerization cycles
- Size-exclusion chromatography (Sephacryl S-200)
Main Results:
- Achieved an average yield of 19 mg of actin per 100 g of pollen.
- Purified pollen actin demonstrated electrophoretic homogeneity with a molecular mass of 42 kDa.
- Amino acid composition and circular dichroism spectra were identical to muscle actin.
- Pollen actin polymerized into F-actin and activated muscle myosin ATPase activity sevenfold.
Conclusions:
- Maize pollen provides a viable source for high-purity actin suitable for biochemical studies.
- Pollen actin shares significant biochemical and functional similarities with muscle actin.
- This purified actin can be utilized to investigate the actomyosin system in higher plants.
