Effect of ligands on Drosophila phosphorylase a as monitored by its enzymic inactivation

Research output: Contribution to journalArticle

Abstract

1. 1. The dephosphorylation of Drosophila phosphorylase a with the catalytic subunit of fruit-fly protein phosphatase-1 was inhibitied by AMP, IMP, ADP, ATP, glucose-6-P, glucose-1-P and UDPG. Glucose, caffeine and glycogen did not influence the reaction. 2. 2. The inhibitory effect of AMP was reduced by glucose and caffeine. 3. 3. The above ligands acted through the modification of phosphorylase a conformation. This conclusion was drawn from the ligands' effect on the dephosporylation of phosphohistone by Drosophila phosphatase-1 and on the tryptic digestion of fruit-fly phosphorylase a.

Original languageEnglish
Pages (from-to)657-659
Number of pages3
JournalInternational Journal of Biochemistry
Volume19
Issue number7
DOIs
Publication statusPublished - 1987

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Phosphorylase a
Drosophila
Adenosine Monophosphate
Ligands
Caffeine
Glucose
Diptera
Fruit
Adenosine Diphosphate Glucose
Fruits
Uridine Diphosphate Glucose
Protein Phosphatase 1
Inosine Monophosphate
Phosphoprotein Phosphatases
Glycogen
Digestion
Catalytic Domain
Adenosine Triphosphate
Phosphoric Monoester Hydrolases
Adenosine Diphosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Effect of ligands on Drosophila phosphorylase a as monitored by its enzymic inactivation. / Dombrádi, V.; Friedrich, P.; Bot, G.

In: International Journal of Biochemistry, Vol. 19, No. 7, 1987, p. 657-659.

Research output: Contribution to journalArticle

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