Partial purification of myosin from lily pollen tubes by monitoring with in vitro motility assay |
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Authors: | Kohno T Ishikawa R Nagata T Kohama K Shimmen T |
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Institution: | (1) Department of Botany, Faculty of Science, University of Tokyo, Hongo, Tokyo;(2) Department of Pharmacology, Gunma University, School of Medicine, Maebashi, Gunma;(3) Department of Life Science, Faculty of Science, Himeji Institute of Technology, 1479-1 Harima Science Park City, 678-12 Hy go, Japan |
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Abstract: | Summary Myosin in pollen tubes ofLilium longiflorum was partially purified, using an in vitro motility assay as a monitor. The main components in the partially purified preparation had molecular masses of 110, 120, and 140 kDa in SDS-PAGE. They became bound to actin filaments in an ATP-dependent manner. Among the components, only that of 120 kDa became bound to ATP and was concluded to be the heavy chain of pollen tube myosin.Abbreviations ATP
adenosine-5 -triphosphate
- DTT
dithiothreitol
- EB
extraction buffer
- EGTA
ethyleneglycol-bis-( -aminoethylether) N, N, N , N -tetraacetic acid
- PAGE
polyacrylamide gel electrophoresis
- PIPES
piperazine-N,N -bis-(2-ethanesulfonic acid)
- PMSF
phenylmethylsulfonyl fluoride
- SDS
sodium dodecylsulfate
- TBS
Tris buffered saline
- TEB
Tris-EGTA buffer |
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Keywords: | Actin Actomyosin In vitro Motility assay Myosin Pollen tube |
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