ArticleThe Journal of cell biology1984
A 45,000-mol-wt protein-actin complex from unfertilized sea urchin egg affects assembly properties of actin.
Article in The Journal of cell biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 44 citations in OpenAlex.
- A novel protein accumulated during maturation of the pods of the plant Impatiens balsamina.Molecular and cellular biochemistry · 1994Article
- Mechanism of the insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin.Journal of muscle research and cell motility · 1991Article
- A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization.The Journal of cell biology · 1989Article
- Probing nucleation, cutting and capping of actin filaments.Journal of muscle research and cell motility · 1989Review
- The purification of a 50 kDa protein-actin complex from unfertilized sea-urchin (Strongylocentrotus purpuratus) eggs.The Biochemical journal · 1989Article
- The 50 kDa protein-actin complex from unfertilized sea-urchin (Strongylocentrotus purpuratus) eggs. Interaction with actin.The Biochemical journal · 1989Article
- Purification of myxamoebal fragmin, and switching of myxamoebal fragmin to plasmodial fragmin during differentiation of Physarum polycephalum.Journal of muscle research and cell motility · 1988Article
- Actin filaments, stereocilia, and hair cells of the bird cochlea. V. How the staircase pattern of stereociliary lengths is generated.The Journal of cell biology · 1988Article
- The effects of a 45 000 molecular weight protein from unfertilized sea urchin eggs and its 1:1 actin complex on actin filaments.Journal of muscle research and cell motility · 1986Article
- Alpha-actinin from sea urchin eggs: biochemical properties, interaction with actin, and distribution in the cell during fertilization and cleavage.The Journal of cell biology · 1985Article
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2 authors.
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Abstract
A one-to-one complex of a 45,000-mol-wt protein and actin was purified from unfertilized eggs of the sea urchin, Hemicentrotus pulcherrimus, by means of DNase l-Sepharose affinity and gel filtration column chromatographies. Effects of the complex on the polymerization of actin were studied by viscometry, spectrophotometry, and electron microscopy. The results are summarized as follows: (a) The initial rate of actin polymerization is inhibited at a very low molar ratio of the complex to actin. (b) Acceleration of the initial rate of polymerization occurs at a relatively high, but still substoichiometric, molar ratio of the complex to actin. (c) Annealing of F-actin fragments is inhibited by the complex. (d) The complex prevents actin filaments from depolymerizing. (e) Growth of the actin filament is inhibited at the barbed end. In all cases except b, a molar ratio of less than 1:100 of the 45,000-mol-wt protein-actin complex to actin is sufficient to produce these significant effects. These results indicate that the 45,000-mol-wt protein-actin complex from the sea urchin egg regulates the assembly of actin by binding to the barbed end (preferred end or rapidly growing end) of the actin filament. The 45,000-mol-wt protein-actin complex can thus be categorized as a capping protein.
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