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Biochemical andmolecular characterization of N66 from the shell of Pinctada mazatlanica
Crisalejandra Rivera Pérez
CATALINA MAGALLANES DOMINGUEZ
Josafat Jehú Ojeda Ramírez de Areyano
NORMA YOLANDA HERNANDEZ SAAVEDRA
Acceso Abierto
Atribución-NoComercial-SinDerivadas
DOI: 10.7717/peerj.7212
ISSN: 21678359
URL: https://peerj.com/articles/7212/
"Mollusk shell mineralization is a tightly controlled process made by shell matrix proteins (SMPs). However, the study of SMPs has been limited to a few model species. In this study, the N66 mRNA of the pearl oyster Pinctada mazatlanica was cloned and functionally characterized. The full sequence of the N66 mRNA comprises 1,766 base pairs, and encodes one N66 protein. A sequence análisis revealed that N66 contained two carbonic anhydrase (CA) domains, a NG domain and several glycosylation sites. The sequence showed similarity to the CA VII but also with its homolog protein nacrein. The native N66 protein was isolated from the Shell and identified by mass spectrometry, the peptide sequence matched to the nucleotide sequence obtained. Native N66 is a glycoprotein with a molecular mass of 60–66 kDa which displays CA activity and calcium carbonate precipitation ability in presence of different salts. Also, a recombinant form of N66 was produced in Escherichia coli, and functionally characterized. The recombinant N66 displayed higher CA activity and crystallization capability than the native N66, suggesting that the lack of posttranslational modifications in the recombinant N66 might modulate its activity. "
PeerJ
2019
Artículo
PeerJ
Inglés
Rivera-Perez C, Magallanes-Dominguez C, Dominguez-Beltran RV, Ojeda-Ramirez de Areyano JJ, Hernandez- Saavedra NY. 2019. Biochemical and molecular characterization of N66 from the shell of Pinctada mazatlanica. PeerJ 7:e7212 DOI 10.7717/peerj.7212
GENÉTICA ANIMAL
Versión publicada
publishedVersion - Versión publicada
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