Proton magnetic resonance studies on SH groups in glycogen phosphorylase b

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Abstract

The reaction between 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB) and the SH groups of glycogen phosphorylase b (α-1,4-glucan:orthophosphate glycosyltransferase, EC 2.4.1.1) has been investigated. The interaction of glycogen phosphorylase b and its allosteric activator AMP was detected by proton magnetic resonance spectroscopy. Specific broadening of the H2 and H8 resonance lines of AMP, caused by the AMP-glycon phosphorylase b interaction, decreased quantitatively upon the DTNB treatment. 60Co γ-irradiation of the enzyme also decreased the AMP-enzyme interaction. It is assumed that SH groups of the glycogen phosphorylase b are involved in AMP binding.

Original languageEnglish
Pages (from-to)191-194
Number of pages4
JournalBBA - Enzymology
Volume315
Issue number1
DOIs
Publication statusPublished - Jul 5 1973

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Phosphorylase b
Glycogen Phosphorylase
Adenosine Monophosphate
Protons
Magnetic Resonance Spectroscopy
Dithionitrobenzoic Acid
Nitrobenzoates
Glycosyltransferases
Enzymes
Phosphates

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Proton magnetic resonance studies on SH groups in glycogen phosphorylase b. / Gáspár, R.; Damjanovich, S.

In: BBA - Enzymology, Vol. 315, No. 1, 05.07.1973, p. 191-194.

Research output: Contribution to journalArticle

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