Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily

Biochem Biophys Res Commun. 1998 Aug 10;249(1):61-5. doi: 10.1006/bbrc.1998.9088.


From lily pollen tubes, an actin-binding protein composed of 115-kDa polypeptide was purified sequentially by co-precipitation method with F-actin, hydroxylapatite column, gel filtration column and DE-52 ion exchange column chromatography. This component displayed a tendency to aggregate in solutions of low ionic strength, indicating a hydrophilic characteristic. Under physiological ionic conditions, this component bound to F-actin in an actin-concentration-dependent was saturable manner. Binding of this component to F-actin was independent of ATP and Ca(2+)-concentrations. Fluorescent microscopy revealed that F-actin labeled with rhodamine-phalloidin showed bundling in the presence of this component. Judging from the lack of antibody cross-reactivity, this component does not seem to be related to alpha-actinin of skeletal muscle and plant 135-kDa actin-bundling protein. Therefore, this component is the F-actin binding protein, which has not been identified thus far in plant cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Liliaceae / metabolism*
  • Microfilament Proteins / isolation & purification*
  • Microfilament Proteins / metabolism*
  • Plant Proteins / isolation & purification*
  • Plant Proteins / metabolism*


  • Actins
  • Microfilament Proteins
  • Plant Proteins