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

Purification of lobster phosphorylase was achieved by a mild method which involves ammonium sulfate and diethylaminoethyl cellulose column chromatography. Both lobster phosphorylase b and a were crystallized by dialysis against 0.01 m EDTA, pH 6.8, which was 30% saturated in ammonium sulfate. Structural and catalytic studies on crystalline lobster phosphorylase are reported. Striking differences from rabbit muscle phosphorylase were found in the amino acid composition, association-dissociation behavior, catalytic efficiency at cold temperature, cold inactivation, energy of activation, and kinetic constants including the allosteric constant. The molecular weight and the extinction coefficient for lobster phosphorylase b are also reported in this study and a model is presented to account for the allosteric properties of this enzyme.

Structural and catalytic properties of lobster muscle glycogen phosphorylase