Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-30446
J Cell Biol 1979 Jul 01;821:212-26. doi: 10.1083/jcb.82.1.212.
Show Gene links Show Anatomy links

Actin in triton-treated cortical preparations of unfertilized and fertilized sea urchin eggs.

Spudich A , Spudich JA .


???displayArticle.abstract???
Triton-treated cortical fragments of unfertilized and fertilized sea urchin eggs prepared in the presence of greater than or equal to 5 mM EGTA contain 15-30% of the total egg actin. However, actin filaments are not readily apparent by electron microscopy on the cortical fragments of unfertilized eggs but are numerous on those of fertilized eggs. The majority of the actin associated with cortical fragments of unfertilized eggs is solubilized by dialysis against a low ionic strength buffer at pH 7.5. This soluble actin preparation (less than 50% pure actin) does not form proper filaments in 0.1 M KCl and 3 mM MgCl2, whereas actin purified from this preparation does, as judged by electron microscopy. Optical diffraction analysis reveals that these purified actin filaments have helical parameters very similar to those of muscle actin. Furthermore, the properties of the purified actin with regard to activation of myosin ATPase are similar to those of actin from other cell types. The possibility that actin is maintained in a nonfilamentous form on the inner surface of the unfertilized egg plasma membrane and is induced to assemble upon fertilization is discussed.

???displayArticle.pubmedLink??? 573270
???displayArticle.pmcLink??? PMC2110418
???displayArticle.link??? J Cell Biol


Genes referenced: LOC100887844 LOC115919910 LOC581395 LOC590297

References [+] :
Ames, Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. 1974, Pubmed