Inactivation and Activation of Liver Phosphorylase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1955-01

AUTHORS

EARL W. SUTHERLAND, WALTER D. WOSILAIT

ABSTRACT

THE level of phosphorylase in liver slices represents a balance between inactivation and resynthesis of the active form; epinephrine and glucagon rapidly increase the amount of active phosphorylase in pre-incubated liver slices1,2. In order to study the nature of the change in the phosphorylase molecule, liver phosphorylase and the enzyme inactivating it from dog liver have been prepared in purified form. The liver phosphorylase was purified approximately 400-fold, a value higher than previously reported3; this purified enzyme was very soluble in water and when inactivated enzymatically showed little or no activity when tested in the presence of adenylic acid. The inactivating enzyme from dog liver was also purified about 400-fold, and this purified enzyme was sufficiently active for microgram quantities to be used in most experiments. Preliminary tests using several proteins as possible substrates have revealed no proteolytic activity. More... »

PAGES

169-170

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/175169a0

DOI

http://dx.doi.org/10.1038/175169a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013034886

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/13235837


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