Glycosylation enhances functional stability of the chemotactic cytokine CCL-2

Autor: Ruggiero P., Flati S., Di Cioccio V., G. Maurizi G., Macchia G., Facchin A., Anacardio R., Maras B., Lucarelli M., Boraschi D.

Publikováno v: European cytokine network (Montrouge) 14 (2003): 91–96.
info:cnr-pdr/source/autori:Ruggiero P., Flati S., Di Cioccio V., G. Maurizi G., Macchia G., Facchin A., Anacardio R., Maras B., Lucarelli M., Boraschi D./titolo:Glycosylation enhances functional stability of the chemotactic cytokine CCL-2./doi:/rivista:European cytokine network (Montrouge)/anno:2003/pagina_da:91/pagina_a:96/intervallo_pagine:91–96/volume:14

The human chemokine CCL2 gene was expressed in the yeast P.pastoris and gave rise to a mixture of differently glycosylated recombinant proteins. In comparison to non-glycosylated E.coli-derived CCL2, glycosylated yeast CCL2L was 4-20 times less activ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::f5f7176d097e4a020ca2df27c3049bfd
https://publications.cnr.it/doc/55758