Open AccessStructural Characterisation of Human Recombinant Glycohormones Follitropin, Lutropin and Choriogonadotropin Expressed in Chinese Hamster Ovary Cells
Author(s) -
Amoresano Angela,
Siciliano Rosa,
Orrù Stefania,
Napoleoni Roberta,
Altarocca Valter,
Luca Eva,
Sirna Antonino,
Pucci Piero
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0608r.x
Subject(s) - chinese hamster ovary cell , recombinant dna , glycan , glycosylation , oligosaccharide , glycoprotein , biochemistry , peptide sequence , biology , chemistry , microbiology and biotechnology , gene , receptor
The α and β chains from human recombinant gonadotropins follitropin, lutropin and choriogonadotropin 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 occurred at the N‐terminus of the follitropin β chain and at the C‐terminus of 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 ‐acetyllactos‐amine repeats on the antennae. The overall structure of the recombinant glycohormones corresponds to their natural counterparts with the exception that sulphated terminal glycosylation is missing.