A large calcium-binding protein associated with the larval spicules of the sea urchin embryo
β Scribed by Mineo Iwata; Eizo Nakano
- Book ID
- 113210988
- Publisher
- Elsevier Science
- Year
- 1986
- Weight
- 922 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0045-6039
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
We have purified and characterized a collagenase/gelatinase activity expressed during sea urchin embryonic development. The native molecular mass was determined to be 160 kDa, while gelatin substrate gel zymography revealed an active species of 41 kDa, suggesting that the native enzyme is a tetramer
## Abstract We have investigated the biochemical and functional properties of toposome, a major protein component of sea urchin eggs and embryos. Atomic force microscopy was utilized to demonstrate that a Ca^2+^βdriven change in secondary structure facilitated toposome binding to a lipid bilayer. T
A new embryonic extracellular matrix protein has been purified from eggs of the sea urchin Paracentrotus lividus. The molecule is a 210 kD dimer consisting of two 105 kD subunits that are held together by S-S bridges. In the unfertilized egg, the protein is found within granules uniformly distribute