Amoresano A, Siciliano R, Orrù S, Napoleoni R, Altarocca V, De Luca E, Sirna A, Pucci P
Servizio di Spettrometria di Massa del CNR, Naples, Italy.
Eur J Biochem. 1996 Dec 15;242(3):608-18. doi: 10.1111/j.1432-1033.1996.0608r.x.
The alpha and beta 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 alpha 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 beta chain and at the C-terminus of the lutropin beta chain. The N-linked glycans from the three beta chains were found to contain fucosylated and sialylated diantennary and triantennary complex-type structures. The follitropin beta chain showed the presence of N-acetyllactosamine 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.
