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Exp Cell Res. 1990 Dec;191(2):219-26.

The association of glycosomal enzymes and microtubules: a physiological phenomenon or an experimental artifact?

Author information

1
Department of Membrane Research, Weizmann Institute of Science, Rehovot, Israel.

Abstract

Subpellicular microtubules isolated from Trypanosoma brucei parasites were fractionated on a phosphocellulose column, and the trypanosomal p52 microtubule-associated protein was eluted along with two other proteins of 41 and 36 kDa. These proteins were found to be the glycosomal enzymes aldolase (41 kDa) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH, 36 kDa) by enzyme activity, antibody cross-reaction, and N-terminal sequencing. These enzymes were coprecipitated with tubulin in the presence of taxol, and aldolase had the capacity to polymerize tubulin and crosslink microtubules. Immunolocalization of anti-aldolase and anti-GAPDH antibodies did not show an interaction between these enzymes and the subpellicular microtubules. The question whether the copurification of aldolase and the subpellicular microtubules could reflect a physiological phenomenon or may be an experimental artifact is discussed.

PMID:
1979542
DOI:
10.1016/0014-4827(90)90008-x
[Indexed for MEDLINE]

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