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

A number of immunological methods have been employed to show that the small subunit of HL-A antigens, isolated either after papain treatment or after solubilization with detergent, is identical to β2 -microglobulin, a protein previously isolated from human urine and shown to be homologous in structure to constant region domains of immunoglobulins. Moreover, quantitative data indicate virtually total identity between the small subunit of HL-A antigens and β2 -microglobulin. Studies of the turnover of labeled HL-A antigens from the lymphocyte surface indicate that the two subunits turn over at similar rates, although only the small subunit could be detected in the culture medium. The significance of these observations is discussed.

Immunological Identity of the Small Subunit of HL-A Antigens and β 2 -Microglobulin and Its Turnover on the Cell Membrane

Immunological Identity of the Small Subunit of HL-A Antigens and β ₂ -Microglobulin and Its Turnover on the Cell Membrane