J Biochem 1981 Sep 01;903:581-7. doi: 10.1093/oxfordjournals.jbchem.a133512.

Evidence that a polysaccharide from the cortex of sea urchin egg inhibits microtubule assembly through its binding to microtubule-associated proteins.

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A new factor that not only inhibits brain microtubule assembly but also causes depolymerization of pre-assembled microtubules was purified from unfertilized sea urchin egg cortices. The purified fraction contained neither proteins nor nucleic acids. The inhibitory activity of the fraction was heat-stable and insensitive to various proteases, but decrease on treatment with glycosidases or with periodic acid. The purified factor was identified as a polysaccharide by analysis of the sugar composition. The sedimentation constant of the factor was estimated to be 9S by sucrose density gradient centrifugation. Polyacrylamide gel electrophoresis of the factor revealed a single broad band stained with periodic acid-Schiff reagent. The factor completely inhibited microtubule assembly at a factor: microtubule protein ratio of 0.03 (w/w). The polysaccharide was found to bind to microtubule-associated proteins, thereby inhibiting microtubule assembly.

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Genes referenced: LOC100887844