scholarly journals Localization of a high-molecular-weight actin binding protein in the sea urchin egg from fertilization through cleavage.

1989 ◽  
Vol 14 (3) ◽  
pp. 363-374 ◽  
Author(s):  
Tomoyoshi Yoshigaki ◽  
Shohei Maekawa ◽  
Sachiko Endo ◽  
Hikoichi Sakai
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sea Urchin ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Sea Urchin Egg

scholarly journals Isolation and Structural Properties of a High-Molecular-Weight Actin-Binding Protein (Filamin-Like Protein) in Hog Thyroid Gland

1982 ◽  
Vol 129 (1) ◽  
pp. 149-155 ◽  
Author(s):  
Claude ROUSTAN ◽  
Mireille BOYER ◽  
Abdellatif FATTOUM ◽  
Rene JEANNEAU ◽  
Yves BENYAMIN ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Thyroid Gland ◽  
High Molecular Weight ◽  
Structural Properties ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia.

1984 ◽  
Vol 98 (5) ◽  
pp. 1611-1618 ◽  
Author(s):  
K Sutoh ◽  
M Iwane ◽  
F Matsuzaki ◽  
M Kikuchi ◽  
A Ikai
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Physarum Polycephalum ◽  
Binding Protein ◽  
High Ionic Strength ◽  
Actin Binding ◽  
Electron Microscopic ◽  
Actin Binding Protein ◽  
Isolation And Characterization

A high molecular weight actin-binding protein was isolated from the Physarum polycephalum plasmodia. The protein ( HMWP ) shares many properties with other high molecular weight actin-binding proteins such as spectrin, actin-binding protein from macrophages, and filamin. It has a potent activity to cross-link F-actin into a gel-like structure. Its cross-linking activity does not depend on calcium concentrations. Hydrodynamic studies have revealed that the protein is in the monomeric state of a polypeptide chain with molecular weight of approximately 230,000 in a high ionic strength solvent, while it self-associates into a dimer under physiological ionic conditions. Electron microscopic examinations of HMWP have shown that the monomer particle observed in a high ionic strength solvent is rod shaped with the two-stranded morphology very similar to that of spectrin. On the other hand, under physiological ionic conditions, the HMWP dimer shows the dumb-bell shape with two globular domains connected with a thin flexible strand.

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