Isolation and characterization of sea urchin toxin

Toxicon ◽  
1965 ◽  
Vol 3 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Charles B. Alender ◽  
George A. Feigen ◽  
Joseph T. Tomita
Keyword(s):  
Sea Urchin ◽  
Isolation And Characterization

Isolation and Characterization of Low Density Detergent-Insoluble Membrane (LD-DIM) Fraction from Sea Urchin Sperm

1999 ◽  
Vol 258 (3) ◽  
pp. 616-623 ◽  
Author(s):  
Kaoru Ohta ◽  
Chihiro Sato ◽  
Tsukasa Matsuda ◽  
Masaru Toriyama ◽  
William J. Lennarz ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Low Density ◽  
Isolation And Characterization ◽  
Sea Urchin Sperm

scholarly journals Isolation and characterization of two forms of a cytoskeleton.

1979 ◽  
Vol 83 (1) ◽  
pp. 109-115 ◽  
Author(s):  
K T Edds
Keyword(s):  
Sea Urchin ◽  
Electron Micrographs ◽  
Actin Filaments ◽  
Three Dimensional ◽  
Strongylocentrotus Droebachiensis ◽  
Major Protein ◽  
Molecular Weights ◽  
Isolation And Characterization ◽  
Filament Bundles

Isolated petaloid coelomocytes from the sea urchin Strongylocentrotus droebachiensis transform to a filopodial morphology in hypotonic media. Electron micrographs of negatively stained Triton-insoluble cytoskeletons show that the petaloid form consists of a loose net of microfilaments while the filopodial form consists of paracrystalline bundles of microfilaments. Actin is the major protein of both forms of the cytoskeleton. Additional polypeptides have molecular weights of approximately 220,000, 64,000, 57,000, and 27,000 daltons. Relative to actin the filopodial cytoskeletons have an average of 2.5 times as much 57k polypeptide as the petaloid cytoskeletons. Treatment with 0.25 M NaCl dissociates the filament bundles into individual actin filaments free of the actin-associated polypeptides. Thus, one or more of these actin-associated polypeptides may be responsible for crosslinking the actin filaments into bundles and maintaining the three-dimensional nature of the cytoskeletons.

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