PMID: 45552Jan 1, 1979

Regulation of avian erythrocyte AMP-deaminase

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
W C Kruckeberg, O P Chilson

Abstract

1. Kinetic data for avian erythrocyte AMP-deaminase in lysate supernatants and 2000-fold purified enzyme were consistent with an allosteric model having four binding sites for substrate. 2. Relative to the purified enzyme, AMP-deaminase in lysate supernatants exhibited a greater S0.5 and enhanced sensitivity toward phytic acid, but was far less sensitive toward potassium ion. 3. In the absence of potassium chloride, the enzymatic activity in lysates exhibited hysteresis at subsaturating 5'-AMP. This response was modified reversibly by allosteric ligands. 4. It is concluded that the characteristics of avian RBC AMP-deaminase, as expressed in lysates, may reflect important intermolecular interactions and better represent the regulatory properties of this enzyme in erythrocytes.

References

Jan 15, 1973·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·H Henry, O P Chilson
Mar 21, 1974·Biochimica Et Biophysica Acta·C Y Lian, D R Harkness
Jun 18, 1974·Biochimica Et Biophysica Acta·T G Brady, J F Costello
May 1, 1965·Journal of Molecular Biology·J MONODJ P CHANGEUX

Citations

Jan 1, 1983·Progress in Biophysics and Molecular Biology·H D EllertonH A Robinson
Jan 1, 1983·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J P Raffin
Jan 1, 1986·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J P Raffin

Related Concepts

Phosphaden
Allosteric Regulation
AMP Deaminase
Ampholytes
Erythrocytes
Hydrogen-Ion Concentration
Nucleotide Deaminases
Phytin
Slow-K

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