Polymerization of Actin from Maize Pollen
| Autor: | Lung-Fei Yen, Shutao Cai, Xiong Liu |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Heavy meromyosin
Physiology Myosin ATPase food and beverages Plant Science macromolecular substances Biology Microfilament biology.organism_classification medicine.disease_cause Actina chemistry.chemical_compound Polymerization chemistry Biochemistry Pollen Genetics Biophysics medicine otorhinolaryngologic diseases Cytochalasin B Actin Research Article |
| Zdroj: | Plant physiology. 107(1) |
| ISSN: | 1532-2548 |
| Popis: | Here we describe the in vitro polymerization of actin from maize (Zea mays) pollen. The purified actin from maize pollen reported in our previous paper (X. Liu, L.F. Yen [1992] Plant Physiol 99: 1151-1155) is biologically active. In the presence of ATP, KCl, and MgCl2 the purified pollen actin polymerized into filaments. During polymerization the spectra of absorbance at 232 nm increased gradually. Polymerization of pollen actin was evidently accompanied by an increase in viscosity of the pollen actin solution. Also, the specific viscosity of pollen F-actin increased in a concentration-dependent manner. The ultraviolet difference spectrum of pollen actin is very similar to that of rabbit muscle actin. The activity of myosin ATPase from rabbit muscle was activated 7-fold by the polymerized pollen actin (F-actin). The actin filaments were visualized under the electron microscope as doubly wound strands of 7 nm diameter. If cytochalasin B was added before staining, no actin filaments were observed. When actin filaments were treated with rabbit heavy meromyosin, the actin filaments were decorated with an arrowhead structure. These results imply that there is much similarity between pollen and muscle actin. |
| Databáze: | OpenAIRE |
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