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Journal of Comparative Physiology B

, Volume 156, Issue 1, pp 77–85 | Cite as

Regulatory features of glycogen phosphorylase from frog brain (Rana temporaria)

  • Günter Kamp
  • Gerhard Wegener
Article

Summary

  1. 1.

    Glycogen content and the activity of glycogen phosphorylase (GPase) are much higher in brain tissue of the Common frog (Rana temporaria) than in brain tissue of mammals and birds (Table 1).

     
  2. 2.

    In phosphate buffer GPase is extracted from frog orain in a form completely active without addition of AMP and has therefore to be regarded as phosphorylase a. Several procedures to extract the b-form of the enzyme from the tissue have been unsuccessful. In resting skeletal muscle predominantly the AMP dependent b-form is present (Table 1).

     
  3. 3.

    In vitro, however, the existence of the complete interconverting system can be demonstrated. If NaF (a phosphatase inhibitor) was omitted from the homogenization medium, GPase activity decreased but concomitantly a significant activation by AMP was observed. The process is reverted under conditions favouring protein phosphorylation (Fig. 1).

     
  4. 4.

    Lowering the AMP concentration by dilution or dialysis of tissue extract also causes a loss of GPase activity, but a different mechanism is involved. This effect is quite specific and based on a dissociation of the dimeric enzyme into subunits (Fig. 4). Reactivation is specifically blocked byl-cysteine (Figs. 2 and 3).

     
  5. 5.

    Both substrates, glycogen andP i, stabilize the enzyme synergistically (Fig. 5).

     
  6. 6.

    At low levels ofP i and AMP, temperature markedly affects the dissociation of the enzyme with the consequence that its catalytic activity is nearly independent of temperature. This might be interpreted as a metabolic adaptation contributing to the ability of the CNS to function over a wide range of temperatures.

     

Keywords

Phosphorylase Tissue Extract Glycogen Content Glycogen Phosphorylase Standard Metabolic Rate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

AMP, ADP, ATP

adenosine 5′-mono-, di-, triphosphate

BSA

bovine serum albumin

CMP

cytidine 5′-monophosphate

EDTA

ethylenediaminetetraacetate

EGTA

ethyleneglycol-bis(2-aminoethylether),N,N′-tetraacetate

GMP

guanosine 5′-monophosphate

GPase

glycogen phosphorylase (EC 2.4.1.1.)

G6PDH

glucose-6-phosphate dehydrogenase (EC 1.1.1.49)

IMP

inosine 5′-monophosphate

NMR

nuclear magnetic resonance

ME

mercaptoethanol

NADP (H)

β-nicotinamide adenine dinucleotide phosphate (reduced)

pCMB

p-chloromercuribenzoate

PEP

phosphoenolpyruvate

PGM

phosphoglucomutase (EC 2.7.5.1)

PFK

phosphofructokinase (EC 2.7.1.11)

PK

pyruvate kinase (EC 2.7.1.40)

PLP

pyridoxal 5′-phosphate

TRA

triethanolamine hydrochloride

TRIS

tris (hydroxymethyl) aminomethane

UMP

uridine 5′-monophosphate

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Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • Günter Kamp
    • 1
  • Gerhard Wegener
    • 1
  1. 1.Institut für Zoologie der Johannes Gutenberg-UniversitätMainzGermany

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