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

The serological and physicochemical properties of the following three forms of human anti-gamma-globulin factors were compared: (a) rheumatoid factors; (b) Milgrom type anti-gamma-globulin factors; and (c) factors directed against an antigen in human gammaG-globulin that is hidden in the intact molecule and revealed by enzymatic digestion at low pH. The property common to these factors is ability to interact with human gammaG-globulin; they are distinguishable because they react with different antigenic groups on this molecule. In all of five sera, the Milgrom type anti-gamma-globulin factors were gammaM-globulins. They reacted with various human gammaG-globulin antibodies but failed to interact with gammaM-globulin type antibodies in agglutination and absorption experiments. When isolated from other anti-gamma-globulin factors, they agglutinated red cells coated with intact anti-Rh antibodies, but failed to react with cells cells coated with pepsin-digested anti-Rh antibody. These observations indicate that the agglutinator reacts with the crystallizable, inert fragment of gammaG-globulin. Anti-gamma-globulin activity directed against an antigen in human gammaG-globulin revealed by pepsin digestion was demonstrated in gammaG-, gammaA-, and gammaM-globulins. This anti-gamma-globulin factor could be absorbed by antigen-antibody precipitates containing human antibody, which shows that the hidden antigen in human gammaG-globulin is revealed not only by enzymatic digestion at low pH, but also when gammaG-globulin is present as antibody in an antigen-antibody precipitate. Rheumatoid factors and Milgrom type anti-gamma-globulin factors were also absorbed by antigen-antibody precipitates containing human antibody. The results indicate that the three distinct forms of antigamma-globulin factors may all be produced as a result of antigenic stimulation by autologous antigen-antibody complexes.

PROPERTIES OF VARIOUS ANTI-γ-GLOBULIN FACTORS IN HUMAN SERA