English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Two populations of immunoglobulin G (IgG) molecules were isolated from pooled rabbit serum. The first was almost devoid of galactosamine and was obtained in a yield of 7% of the total IgG; the second contained on average a single residue of galactosamine per molecule and was obtained in a yield of 30% of the total IgG. The galactosamine, which is present solely in the C2-oligosaccharide, appeared to be present on one H-chain and not the other in the four-chain structure. Evidence was obtained by the isolation of a glycopeptide linked through a disulphide bridge to a second peptide of the same sequence; the oligosaccharide attached to the first peptide was absent from the complementary peptide. Further evidence was obtained by degradation and analysis of the 5S IgG fragment, which comprises an intact half-molecule coupled through a disulphide bridge to the Fc fragment derived from the opposing half molecule (Goodman, 1965); only the intact H-chain carried the C2-oligosaccharide.

The oligosaccharide units of rabbit immunoglobulin G. Asymmetric attachment of C2-oligosaccharide