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 language | English (US) |
|---|---|
| Pages (from-to) | 139-152 |
| Number of pages | 14 |
| Journal | Annals of the New York Academy of Sciences |
| Volume | Vol. 210 |
| State | Published - 1973 |
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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 journal › Article
}
TY - JOUR
T1 - Physicochemical and catalytic properties of crystallized human muscle glycogen phosphorylase
AU - Assaf, S. A.
AU - Yunis, Adel A
PY - 1973
Y1 - 1973
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0015690670&partnerID=8YFLogxK
M3 - Article
VL - Vol. 210
SP - 139
EP - 152
JO - Annals of the New York Academy of Sciences
JF - Annals of the New York Academy of Sciences
SN - 0077-8923
ER -