Interaction of ligands in phosphorylase A as monitored by crosslinking and enzymatic modifications: Synergism of glucose and caffeine manifested in the exposure of N-terminal segment

V. Dombrádi, B. Tóth, G. Bot, J. Hajdu, P. Friedrich

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6 Citations (Scopus)

Abstract

1. 1. Glycogen, caffeine and glucose dissociate phosphorylase a tetramer to dimers with half-maximum effect at 0.16%, 1.1 and 71 mM concentration, respectively, as monitored by crosslinking with dimethyl suberimidate at 18°C. 2. 2. The above ligands increase the rate of dephosphorylation and tryptic digestion of phosphorylase a at 18°C in the same way with half-maximum effect at 0.04%, 0.1 and 9 mM concentration, respectively. 3. 3. Caffeine and glucose acted synergistically in tetramer dissociation as well as in the enzymic modifications. 4. 4. The α-anomer of d-glucose was twice as effective as its mutarotational equilibrium solution.

Original languageEnglish
Pages (from-to)277-284
Number of pages8
JournalInternational Journal of Biochemistry
Volume14
Issue number4
DOIs
Publication statusPublished - 1982

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Phosphorylases
Caffeine
Phosphorylase a
Crosslinking
Ligands
Glucose
Dimethyl Suberimidate
Glycogen
Dimers
Digestion

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Interaction of ligands in phosphorylase A as monitored by crosslinking and enzymatic modifications: Synergism of glucose and caffeine manifested in the exposure of N-terminal segment",
abstract = "1. 1. Glycogen, caffeine and glucose dissociate phosphorylase a tetramer to dimers with half-maximum effect at 0.16{\%}, 1.1 and 71 mM concentration, respectively, as monitored by crosslinking with dimethyl suberimidate at 18°C. 2. 2. The above ligands increase the rate of dephosphorylation and tryptic digestion of phosphorylase a at 18°C in the same way with half-maximum effect at 0.04{\%}, 0.1 and 9 mM concentration, respectively. 3. 3. Caffeine and glucose acted synergistically in tetramer dissociation as well as in the enzymic modifications. 4. 4. The α-anomer of d-glucose was twice as effective as its mutarotational equilibrium solution.",
author = "V. Dombr{\'a}di and B. T{\'o}th and G. Bot and J. Hajdu and P. Friedrich",
year = "1982",
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TY - JOUR

T1 - Interaction of ligands in phosphorylase A as monitored by crosslinking and enzymatic modifications

T2 - Synergism of glucose and caffeine manifested in the exposure of N-terminal segment

AU - Dombrádi, V.

AU - Tóth, B.

AU - Bot, G.

AU - Hajdu, J.

AU - Friedrich, P.

PY - 1982

Y1 - 1982

N2 - 1. 1. Glycogen, caffeine and glucose dissociate phosphorylase a tetramer to dimers with half-maximum effect at 0.16%, 1.1 and 71 mM concentration, respectively, as monitored by crosslinking with dimethyl suberimidate at 18°C. 2. 2. The above ligands increase the rate of dephosphorylation and tryptic digestion of phosphorylase a at 18°C in the same way with half-maximum effect at 0.04%, 0.1 and 9 mM concentration, respectively. 3. 3. Caffeine and glucose acted synergistically in tetramer dissociation as well as in the enzymic modifications. 4. 4. The α-anomer of d-glucose was twice as effective as its mutarotational equilibrium solution.

AB - 1. 1. Glycogen, caffeine and glucose dissociate phosphorylase a tetramer to dimers with half-maximum effect at 0.16%, 1.1 and 71 mM concentration, respectively, as monitored by crosslinking with dimethyl suberimidate at 18°C. 2. 2. The above ligands increase the rate of dephosphorylation and tryptic digestion of phosphorylase a at 18°C in the same way with half-maximum effect at 0.04%, 0.1 and 9 mM concentration, respectively. 3. 3. Caffeine and glucose acted synergistically in tetramer dissociation as well as in the enzymic modifications. 4. 4. The α-anomer of d-glucose was twice as effective as its mutarotational equilibrium solution.

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