Evaluation of in vivo bioactivities of recombinant hypo- (FSH^21/18) and fully- (FSH²⁴) glycosylated human FSH glycoforms in Fshb null mice.

ABSTRACT: The hormone - specific FSHβ subunit of the human FSH heterodimer consists of N-linked glycans at Asn⁷ and Asn²⁴ residues that are co-translationally attached early during subunit biosynthesis. Differences in the number of N-glycans (none, one or two) on the human FSHβ subunit contribute to macroheterogeneity in the FSH heterodimer. The resulting FSH glycoforms are termed hypo-glycosylated (FSH^21/18, missing either an Asn²⁴ or Asn⁷ N-glycan chain on the β - subunit, respectively) or fully glycosylated (FSH²⁴, possessing of both Asn⁷ and Asn²⁴ N-linked glycans on the β - subunit) FSH. The recombinant versions of human FSH glycoforms (FSH^21/18 and FSH²⁴) have been purified and biochem

SUBMITTER: Wang H 

PROVIDER: S-EPMC5048586 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature