The effect of phospholipid bilayers on amp-deaminase from rat tissues

Prus, E; Zydowo, M

doi:10.1016/0020-711x(83)90233-1

Cited by 6 publications

(1 citation statement)

References 15 publications

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“…Hence the precise regulation of heart AMP deaminase activity as a possible modulator of cellular adenosine levels is of great physiological importance and commands growing attention. Surprisingly, isolated skeletal muscle AMP deaminase was found to be sensitive to the ATP-activating effect at very low, non-physiological, concentrations of K+ only [5,6]. A search for ATP-activated AMP deaminase in the heart led us to isolate in 1978 a substrate-specific pig heart AMP deaminase, which is activated by ATP even in the presence of a high K+ concentration (150 mM) [7].…”

Section: Introductionmentioning

confidence: 99%

The interaction of phospholipid bilayers with pig heart AMP deaminase: Fourier-transform infrared spectroscopic and kinetic studies

Tanfani

Kossowska

Purzycka-Preis

et al. 1993

Biochemical Journal

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The interaction of pig heart AMP deaminase with different chemical species of phosphatidylcholine and with natural plasma membranes has been investigated. Phospholipids added to the system either as natural biological membranes (plasma membrane vesicles) or in the form of liposomes containing unsaturated phosphatidylcholine considerably enhanced AMP deaminase activity. The secondary structure of pig heart AMP deaminase in the absence and in the presence of dioleoyl phosphatidylcholine and dipalmitoyl phosphatidylcholine liposomes was investigated by Fourier-transform infrared spectroscopy. Quantitative analysis of the amide I band showed that the enzyme contains 45% beta-sheets, 28% alpha-helix, 16% turns and 11% non-ordered structure. In the presence of dioleoyl phosphatidylcholine liposomes, the beta/alpha content ratio decreased; this decrease was dependent on the amount of lipid added. This phenomenon was not observed in the case of dipalmitoyl phosphatidylcholine liposomes. These data suggest a possible role for membrane phospholipids in the regulation of AMP deaminase activity.

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Section: Introductionmentioning

confidence: 99%