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ECB-ART-35886
Biochim Biophys Acta 1994 Aug 17;12072:194-200. doi: 10.1016/0167-4838(94)00075-1.
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Purification of a low molecular weight microtubule binding protein from sea urchin eggs.

Maekawa S , Mishima M , Toriyama M , Sakai H .


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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.

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Genes referenced: LOC100887844 LOC115919910 tubgcp2