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

Phospho-dephosphohybrids of rabbit skeletal muscle phosphorylase (EC 2.4.1.1; alpha-1,4-glucan: orthophosphate glucosyl transferase) have been prepared and stabilized by attachment to Sepharose activated by cyanogen bromide. They can be distinguished from phosphorylase a by their sensitivity to inhibition by glucose-6-phosphate and activation by adenosine 5'-monophosphate. Stable hybrids have also been formed between phosphorylase subunits containing the active cofactor pyridoxal-phosphate and inactive analogs (pyridoxalphosphate monomethylester or the corresponding reduced compounds). After complete dissociation to monomers, the Sepharose-bound phosphorylase had a residual activity of less than 3% of that of the original matrix-bound dimeric enzyme. The hybrid enzyme is composed of a potentially active subunit containing pyridoxal-phosphate and an intrinsically inactive subunit carrying the analog, and it had half the activity of the original dimeric enzyme. Thus, the interaction of the inactive subunit with matrix-bound phosphorylase monomers elicited activity in the monomers.

Interactions between Native and Chemically Modified Subunits of Matrix-Bound Glycogen Phosphorylase