Pregled bibliografske jedinice broj: 253849
Caspartin: Thermal Stability and Occurrence on Mollusc Calcified Tissues
Caspartin: Thermal Stability and Occurrence on Mollusc Calcified Tissues // THE 9TH INTERNATIONAL SYMPOSIUM ON BIOMINERALIZATION “ ; FROM PALEONTOLOGY TO MATERIALS SCIENCE” ; / Arias, Jose L. (ur.).
Pucón: University of Chile and CIMAT, Santiago, Chile, 2005. str. - (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 253849 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Caspartin: Thermal Stability and Occurrence on Mollusc Calcified Tissues
Autori
Marin, Frederic ; Morin, Virginie ; Knap, Fred ; Guichard, Nathalie ; Marie, Benjamin ; Luquet, Gilles ; Westbroek, Peter ; Medakovic, Davorin
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
THE 9TH INTERNATIONAL SYMPOSIUM ON BIOMINERALIZATION “ ; FROM PALEONTOLOGY TO MATERIALS SCIENCE” ;
/ Arias, Jose L. - Pucón : University of Chile and CIMAT, Santiago, Chile, 2005
Skup
THE 9TH INTERNATIONAL SYMPOSIUM ON BIOMINERALIZATION “ ; FROM PALEONTOLOGY TO MATERIALS SCIENCE” ;
Mjesto i datum
Pucón, Čile, 06.12.2005. - 09.12.2005
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
Pinna nobilis; Shell; Acidic intercrystalline proteins; Thermal stability; ELISA; dot-blot; Western-blot
Sažetak
The Mediterranean fan mussel Pinna nobilis secretes a two-layered shell, the external layer of which is composed of long calcite needles, the prisms. The dissolution of these needles with dilute acetic acid release a remarkable assemblage of acidic intracrystalline proteins, among which caspartin, a 17 kDa aspartic acid-rich protein (Marin et al., 2005). A polyclonal antibody was raised againstcaspartin and used for two purposes: -to checjk the thermal stability of caspartin ; to investigate its presence, or the presence of immunologicaly-related protein, in the calcified tissued of several molluscs. In the first case, prisms of Pinna nobilis were heated at different temperatures, for increasing durations. The degradation of caspartin was followed on SDSPAGE and on Western-blot. The experiments show that caspartinis stable at 100 C degree, but degrades more rapidly at 120 C degree. For the second purpose, EDTA-soluble matrices were extracted from numerous molluscs shells including bivalves, gastropods and cephalopods. These matrices were subsequently tested by ELISA, dot-blot, and Western-blot, to check the presence of caspartin or immunologically-related proteins. The pattern does not follow the phylogeny of molluscs nor it is correlated with the shell microstructural pattern.
Izvorni jezik
Engleski
Znanstvena područja
Fizika, Geologija, Biologija
POVEZANOST RADA
Projekti:
MZOS-0098111 - Mehanizam dugoročnih promjena u ekosustavu Jadranskog mora (Degobbis, Danilo, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Davorin Medaković
(autor)
