Purification of a low molecular weight microtubule binding protein from sea urchin eggs.
A low molecular weight microtubule binding protein(SU-MAP34) was purified from sea urchin eggs. This protein bound strongly to the microtubule formed from purified echinoderm tubulin but showed no cross-linking of microtubules. Monospecific antibody against SU-MAP34 was produced and an immunoblotting analysis showed that this protein was not a breakdown product of a protein of a higher molecular mass. Whole cell staining and confocal laser scanning microscope observation showed that SU-MAP34 localized on the filamentous structure of mitotic apparatus and this structure was identified as the microtubule with double staining using anti-SU-MAP34 and anti-tubulin. An immunoblotting experiment showed an enrichment of SU-MAP34 in a microtubule protein fraction prepared using taxol from a crude extract of the cell.
Maekawa
S
S
Graduate School, Division of Science, University of Tokyo, Japan.
Mishima
M
M
Toriyama
M
M
Sakai
H
H
D000818:Animals; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D015151:Immunoblotting; D008856:Microscopy, Fluorescence; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D010063:Ovum / Q000737:chemistry*; D017239:Paclitaxel / Q000494:pharmacology; D012617:Sea Urchins; D014404:Tubulin / Q000378:metabolism
D008869:Microtubule-Associated Proteins; D014404:Tubulin; D017239:Paclitaxel