The interaction of phospholipid bilayers with pig heart AMP deaminase: Fourier-transform infrared spectroscopic and kinetic studies
Autor: | M M Zydowo, J Purzycka-Preis, Fabio Tanfani, E Kossowska, Michal Wozniak, E. Tartaglini, Enrico Bertoli |
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Rok vydání: | 1993 |
Předmět: |
1
2-Dipalmitoylphosphatidylcholine Spectrophotometry Infrared Swine AMP deaminase activity Adenylyl Imidodiphosphate Lipid Bilayers Phospholipid Synthetic membrane Biochemistry Protein Structure Secondary AMP Deaminase chemistry.chemical_compound Adenosine Triphosphate Phosphatidylcholine Animals Molecular Biology Phospholipids Liposome Fourier Analysis Myocardium AMP deaminase Biological membrane Cell Biology Kinetics Membrane chemistry Phosphatidylcholines lipids (amino acids peptides and proteins) Research Article |
Zdroj: | Biochemical Journal. 291:921-926 |
ISSN: | 1470-8728 0264-6021 |
DOI: | 10.1042/bj2910921 |
Popis: | 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. |
Databáze: | OpenAIRE |
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