Limited proteolysis of glycogen phosphorylase a by subtilisin bpn'

V. Dombrádi, B. Tóth, P. Gergely, G. Bot

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a was undertaken with subtilisin BPN' immobilized to Sepharose 4B. The effect of substrates, activators and inhibitors of phosphorylase a was investigated by monitoring the changes in phosphorylase activity in the SDS gel electrophoretic pattern and in the 32P-content of 32P-labeled phosphorylase a. 2. 2. Phosphorylase a loses its activity upon subtilisin treatment. All ligands tested protect phosphorylase a activity against subtilisin action, probably by inducing structural changes in the tower loop of the enzyme. 3. 3. Glucose-6-P significantly accelerates [32P]peptide release from phosphorylase a through altering the structure of the N-terminal tail segment. 4. 4. The two subunits of dimeric phosphorylase a are held together by strong interactions-deduced from the correlation of the rate of proteolysis and the disappearance of catalytic activity.

Original languageEnglish
Pages (from-to)1329-1336
Number of pages8
JournalInternational Journal of Biochemistry
Volume15
Issue number11
DOIs
Publication statusPublished - 1983

Fingerprint

Phosphorylase a
Proteolysis
Glycogen Phosphorylase
Subtilisin
Subtilisins
Phosphorylases
Sepharose
Towers
Muscle
Tail
Catalyst activity
Skeletal Muscle
Gels
Rabbits
Ligands
Glucose
Peptides
Monitoring
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Limited proteolysis of glycogen phosphorylase a by subtilisin bpn'. / Dombrádi, V.; Tóth, B.; Gergely, P.; Bot, G.

In: International Journal of Biochemistry, Vol. 15, No. 11, 1983, p. 1329-1336.

Research output: Contribution to journalArticle

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N2 - 1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a was undertaken with subtilisin BPN' immobilized to Sepharose 4B. The effect of substrates, activators and inhibitors of phosphorylase a was investigated by monitoring the changes in phosphorylase activity in the SDS gel electrophoretic pattern and in the 32P-content of 32P-labeled phosphorylase a. 2. 2. Phosphorylase a loses its activity upon subtilisin treatment. All ligands tested protect phosphorylase a activity against subtilisin action, probably by inducing structural changes in the tower loop of the enzyme. 3. 3. Glucose-6-P significantly accelerates [32P]peptide release from phosphorylase a through altering the structure of the N-terminal tail segment. 4. 4. The two subunits of dimeric phosphorylase a are held together by strong interactions-deduced from the correlation of the rate of proteolysis and the disappearance of catalytic activity.

AB - 1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a was undertaken with subtilisin BPN' immobilized to Sepharose 4B. The effect of substrates, activators and inhibitors of phosphorylase a was investigated by monitoring the changes in phosphorylase activity in the SDS gel electrophoretic pattern and in the 32P-content of 32P-labeled phosphorylase a. 2. 2. Phosphorylase a loses its activity upon subtilisin treatment. All ligands tested protect phosphorylase a activity against subtilisin action, probably by inducing structural changes in the tower loop of the enzyme. 3. 3. Glucose-6-P significantly accelerates [32P]peptide release from phosphorylase a through altering the structure of the N-terminal tail segment. 4. 4. The two subunits of dimeric phosphorylase a are held together by strong interactions-deduced from the correlation of the rate of proteolysis and the disappearance of catalytic activity.

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