ArticlePlant physiology1992
Purification and characterization of actin from maize pollen.
Article in Plant physiology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 51 citations in OpenAlex.
- Cytoskeletal control of development and environmental adaptation in plants.Science China. Life sciences · 2026Review
- Control of the Actin Cytoskeleton Within Apical and Subapical Regions of Pollen Tubes.Frontiers in cell and developmental biology · 2020Review
- Actin and actin-binding proteins in higher plants.Protoplasma · 2001Review
- Latrunculin B has different effects on pollen germination and tube growth.The Plant cell · 1999Article
- Actin Purified from Maize Pollen Functions in Living Plant Cells.The Plant cell · 1997Article
- Polymerization of Actin from Maize Pollen.Plant physiology · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pollen is an excellent source of actin for biochemical and physiological studies of the actomyosin system in higher plants. We have developed an efficient method to prepare relatively high levels of actin from the pollen of maize (Zea mays L.). The procedures of purification include acetone powder preparation, saturated ammonium sulfate fractionation, diethylaminoethyl-cellulose chromatography, a cycle of polymerization-depolymerization, and Sephacryl S-200 gel filtration. The average yield of actin is 19 milligrams per 100 grams of pollen grains extracted. This is comparable with those of Acanthamoeba castellanii and human platelets. The purified pollen actin is electrophoretically homogeneous and its molecular mass is 42 kilodaltons. The amino acid composition and circular dichroism spectrum of pollen actin are identical to those of muscle actin. The actin purified from pollen is able to polymerize to F-actin. The pollen F-actin activated the activity of the muscle myosin ATPase sevenfold.
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Registered trials
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