| Autor: |
Amoresano, Angela, Siciliano, Rosa, Orrú, Stefania, Napoleoni, Roberta, Altarocca, Valter, De Luca, Eva, Sirna, Antonino, Pucci, Piero |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 12/15/96, Vol. 242 Issue 3, p608-618, 11p |
| Abstrakt: |
The α and β chains from human recombiant gonadotropins follitropin, lutropin ad pin expressed in CHO cells have been structurally characterised both at the protein and at the carbohydrate level by using advanced mass spectrometric procedures. The three α chains share the same amino acid sequence while they display different glycosylation patterns. The oligosaccharide structures detected belong to the complex-type glycans with different degree of sialylation. Partial proteolytic processing occured at the N-terminus of the follitropin β chain and at the C-terminus the lutropin β chain. The N-linked glycans from the three β chains were found to contain fucosylated and sialylated diantennary and triantennary complex-type structures. The follitropin β chain showed the presence of N-acetyllactosamine repeats Oil tile antennae. The overall structure of the recombinant glycolhormones corresponds to their natural counterparts with the exception that sulphated terminal glycosylation is missing. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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