A primer independent activity of rabbit muscle phosphorylase b
Rabbit muscle phosphorylase b was found to be capable of forming protein bound ±-1,4 glucosyl chains upon incubation of the enzyme with appropriate concentrations of glucose-1-phosphate with no primer addition (unprimed synthesis). This activity would only be present in a small fraction of the total...
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todo:paper_03008177_v16_n2-3_p141_Tandecarz2023-10-03T15:17:43Z A primer independent activity of rabbit muscle phosphorylase b Tandecarz, J. Lavintman, N. Cardini, C.E. glucose phosphate glycogen phosphorylase b in vitro study muscle theoretical study Animal Glycogen Hydrogen-Ion Concentration Kinetics Muscles Phosphorylases Rabbits Structure-Activity Relationship Rabbit muscle phosphorylase b was found to be capable of forming protein bound ±-1,4 glucosyl chains upon incubation of the enzyme with appropriate concentrations of glucose-1-phosphate with no primer addition (unprimed synthesis). This activity would only be present in a small fraction of the total muscle phosphorylase b activity, as judged from the high concentrations of enzyme which are required to demonstrate the occurrence of unprimed synthesis. Polyacrylamide gel electrophoresis shows the presence of a phosphorylase isoenzyme capable of accepting glucosyl moieties, giving rise to a glucosylated protein enzymatically active in the chain lengthening of its own glucan. © 1977 Dr. W. Junk b.v. Publishers. Fil:Tandecarz, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Lavintman, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p141_Tandecarz |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
glucose phosphate glycogen phosphorylase b in vitro study muscle theoretical study Animal Glycogen Hydrogen-Ion Concentration Kinetics Muscles Phosphorylases Rabbits Structure-Activity Relationship |
| spellingShingle |
glucose phosphate glycogen phosphorylase b in vitro study muscle theoretical study Animal Glycogen Hydrogen-Ion Concentration Kinetics Muscles Phosphorylases Rabbits Structure-Activity Relationship Tandecarz, J. Lavintman, N. Cardini, C.E. A primer independent activity of rabbit muscle phosphorylase b |
| topic_facet |
glucose phosphate glycogen phosphorylase b in vitro study muscle theoretical study Animal Glycogen Hydrogen-Ion Concentration Kinetics Muscles Phosphorylases Rabbits Structure-Activity Relationship |
| description |
Rabbit muscle phosphorylase b was found to be capable of forming protein bound ±-1,4 glucosyl chains upon incubation of the enzyme with appropriate concentrations of glucose-1-phosphate with no primer addition (unprimed synthesis). This activity would only be present in a small fraction of the total muscle phosphorylase b activity, as judged from the high concentrations of enzyme which are required to demonstrate the occurrence of unprimed synthesis. Polyacrylamide gel electrophoresis shows the presence of a phosphorylase isoenzyme capable of accepting glucosyl moieties, giving rise to a glucosylated protein enzymatically active in the chain lengthening of its own glucan. © 1977 Dr. W. Junk b.v. Publishers. |
| format |
JOUR |
| author |
Tandecarz, J. Lavintman, N. Cardini, C.E. |
| author_facet |
Tandecarz, J. Lavintman, N. Cardini, C.E. |
| author_sort |
Tandecarz, J. |
| title |
A primer independent activity of rabbit muscle phosphorylase b |
| title_short |
A primer independent activity of rabbit muscle phosphorylase b |
| title_full |
A primer independent activity of rabbit muscle phosphorylase b |
| title_fullStr |
A primer independent activity of rabbit muscle phosphorylase b |
| title_full_unstemmed |
A primer independent activity of rabbit muscle phosphorylase b |
| title_sort |
primer independent activity of rabbit muscle phosphorylase b |
| url |
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p141_Tandecarz |
| work_keys_str_mv |
AT tandecarzj aprimerindependentactivityofrabbitmusclephosphorylaseb AT lavintmann aprimerindependentactivityofrabbitmusclephosphorylaseb AT cardinice aprimerindependentactivityofrabbitmusclephosphorylaseb AT tandecarzj primerindependentactivityofrabbitmusclephosphorylaseb AT lavintmann primerindependentactivityofrabbitmusclephosphorylaseb AT cardinice primerindependentactivityofrabbitmusclephosphorylaseb |
| _version_ |
1807317343387254784 |