Adenosine 3',5'-cyclic monophosphate (CAMP) binds t o high-molecular substances which are probably proteins, in homogenates of sea urchin eggs and embryos. The bound CAMP is exchangeable. Optimal pH for the binding capacity of the proteins with CAMP is 4.0, and is shifted t o 5.0 in the presence of
Metal-binding proteins in eggs of various sea urchin species.
✍ Scribed by R. Scudiero; C. Capasso; P.P. De Prisco; A. Capasso; S. Filosa; E. Parisi
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 325 KB
- Volume
- 18
- Category
- Article
- ISSN
- 1065-6995
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✦ Synopsis
Abstract
Metallothionein presence and amount were determined in the unfertilized eggs of six sea urchin species by silver saturation assay and gel‐chromatography of cell extracts. The results showed high levels of metallothionein in the egg cytoplasm of the two Mediterranean species Paracentrotus lividus and Sphaerechinus granularis. No metallothionein was found either in the eggs of Arbacia lixula, or in those of the three Eastern species Strongylocentrotus intermedius, Temnopleurus hardwickii and Clypeaster japonicus. However, the extracts of the latter three species revealed the presence of zinc bound in a macromolecular form, thus suggesting the existence of metal‐binding proteins distinct from metallothioneins.
📜 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