Muscle-type tropomyosin of sea urchin egg increases the actin-binding of nonmuscle-type tropomyosin
Tropomyosin isoforms in eggs of several species of sea urchins are classified into two types, muscle-type and nonmuscle-type, based on their antigenicities. Their actin-binding abilities were investigated using muscle-type isoform (32K) and nonmuscle-type isoform (30K), which were purified by the me...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1996-11, Vol.120 (5), p.922-928 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Tobita, T Hiraide, F Miyazaki, J Ishimoda-Takagi, T |
| description | Tropomyosin isoforms in eggs of several species of sea urchins are classified into two types, muscle-type and nonmuscle-type, based on their antigenicities. Their actin-binding abilities were investigated using muscle-type isoform (32K) and nonmuscle-type isoform (30K), which were purified by the method previously reported and separated by isoelectric focusing from eggs of sea urchin, Strongylocentrotus intermedius. Co-sedimentation assays revealed that 32K could stoichiometrically bind to actin filaments independently of the 30K, but 30K alone bound very poorly. The actin-binding of 30K was, however, considerably increased in the presence of 32K, and the molar ratio of the bound 30K and 32K was approximately 1:1. The increase in the actin-binding of 30K is probably caused by the interaction of 30K with 32K in a head-to-tail manner, as indicated by the higher specific viscosity of the mixture than that of 32K alone. |
| format | Article |
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Their actin-binding abilities were investigated using muscle-type isoform (32K) and nonmuscle-type isoform (30K), which were purified by the method previously reported and separated by isoelectric focusing from eggs of sea urchin, Strongylocentrotus intermedius. Co-sedimentation assays revealed that 32K could stoichiometrically bind to actin filaments independently of the 30K, but 30K alone bound very poorly. The actin-binding of 30K was, however, considerably increased in the presence of 32K, and the molar ratio of the bound 30K and 32K was approximately 1:1. 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| ispartof | Journal of biochemistry (Tokyo), 1996-11, Vol.120 (5), p.922-928 |
| issn | 0021-924X |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry |
| subjects | Actins - metabolism Animals Electrophoresis, Polyacrylamide Gel Isoelectric Focusing Marine Molecular Weight Oocytes - metabolism Sea Urchins Strongylocentrotus intermedius Tropomyosin - metabolism Viscosity |
| title | Muscle-type tropomyosin of sea urchin egg increases the actin-binding of nonmuscle-type tropomyosin |
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