Increased FSH receptor-binding activity observed with N56dg-a:eFSH(b hybrid preparations as compared with the corresponding intact a:eFSH@ hybrid preparations was modest. This may help to explain the conflicting reports on the influence of haAsn52 oligosaccharide on recombinant hFSH binding to its receptor . As these recombinant hFSH preparations were expressed in three different cell lines, i.e., COS-7 monkey kidney cells , Chinese hamster ovary cells , and 293 human embryonic kidney cells , different glycosylation patterns likely resulted from cell-specific differences in oligosaccharide processing. buy ampicillin
Changes in immunoac-tivity due to altered glycosylation are generally ignored, yet may be significant . More importantly, the difference in magnitude of the negative inhibition, caused by increased length of the Asn56 oligosaccharide Man(al-6)Man antenna between eFSHp hybrids and those possessing either an eLHp or an eCGp subunit, suggested a different orientation of these naturally occurring FSH analogues in the FSH receptor from that observed for FSH.