Physicochemical and catalytic properties of crystallized human muscle glycogen phosphorylase

S. A. Assaf, Adel A Yunis

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Studies on human muscle phosphorylase have revealed some differences from the rabbit muscle enzyme not previously appreciated. These include the greater stability of the human enzyme to freezing and storage, its relative resistance to inactivation by 5,5' dithiobis(2 nitrobenzoic acid), and its association dissociation behavior. Perhaps most significant is the greater tendency of human phosphorylase a to dissociate to active dimers than of rabbit phosphorylase a, which remains in tetrameric form even at low enzyme concentration. This suggests that the regulation of phosphorylase activity through the association and dissociation of its subunit structure is species dependent, and that this regulatory mechanism appears to be more sensitive in the human muscle.

Original languageEnglish (US)
Pages (from-to)139-152
Number of pages14
JournalAnnals of the New York Academy of Sciences
VolumeVol. 210
StatePublished - 1973

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Glycogen Phosphorylase
Phosphorylase a
Muscle
Phosphorylases
Muscles
Enzymes
Association reactions
Dithionitrobenzoic Acid
Rabbits
Enzyme Stability
Freezing
Dimers
Thermodynamic properties
Rabbit
Dissociation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Physicochemical and catalytic properties of crystallized human muscle glycogen phosphorylase. / Assaf, S. A.; Yunis, Adel A.

In: Annals of the New York Academy of Sciences, Vol. Vol. 210, 1973, p. 139-152.

Research output: Contribution to journalArticle

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