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

Relatively simple and rapid procedures are described for the large-scale preparation of liver membranes that contain virtually all of the high affinity insulin-binding activity of liver homogenates. The presumed insulin recepotr, which is extracted from these membranes in soluble form with Triton X-100, can be further purified by ammonium sulfate fractionation (3-fold purification) or by diethylaminoethyl-cellulose chromatography (60-fold purification). Several insulin-agarose derivatives have been synthesized that can efficiently extract the insulin-binding protein from the detergent extracts of the membranes. The receptor macro-molecule can be eluted from the affinity columns in high (50-80%) yield by use of urea-containing buffers of moderately low pH. The receptor, thus purified by small-scale affinity chromatography experiments, approaches theoretical purity on the basis of its specific activity. This protein is purified about 250,000-fold from the liver homogenate by detergent extraction and affinity chromatography.

Affinity Chromatography and Purification of the Insulin Receptor of Liver Cell Membranes