Literature DB >> 8489518

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

F Tanfani1, E Kossowska, J Purzycka-Preis, M M Zydowo, M Wozniak, E Tartaglini, E Bertoli.   

Abstract

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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Year:  1993        PMID: 8489518      PMCID: PMC1132457          DOI: 10.1042/bj2910921

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  22 in total

1.  Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water.

Authors:  Y N Chirgadze; O V Fedorov; N P Trushina
Journal:  Biopolymers       Date:  1975-04       Impact factor: 2.505

2.  Modified reagents for determination of urea and ammonia.

Authors:  A L CHANEY; E P MARBACH
Journal:  Clin Chem       Date:  1962-04       Impact factor: 8.327

3.  Examination of the secondary structure of proteins by deconvolved FTIR spectra.

Authors:  D M Byler; H Susi
Journal:  Biopolymers       Date:  1986-03       Impact factor: 2.505

4.  Stabilization of adenylate energy charge by the adenylate deaminase reaction.

Authors:  A G Chapman; D E Atkinson
Journal:  J Biol Chem       Date:  1973-12-10       Impact factor: 5.157

5.  Solubilization of a calcium dependent adenosine triphosphatase from rat heart sarcolemma.

Authors:  N S Dhalla; M B Anand-Srivastava; B S Tuana; R L Khandelwal
Journal:  J Mol Cell Cardiol       Date:  1981-04       Impact factor: 5.000

6.  The effect of phospholipid bilayers on AMP-deaminase from rat tissues.

Authors:  E Prus; M Zydowo
Journal:  Int J Biochem       Date:  1983

7.  The role of adenosine monophosphate nucleosidase in the regulation of adenine nucleotide levels in Azotobacter vinelandii during aerobic-anaerobic transitions.

Authors:  H B Leung; V L Schramm
Journal:  Arch Biochem Biophys       Date:  1978-09       Impact factor: 4.013

8.  An improved purification, crystallization, and some properties of rabbit muscle 5'-adenylic acid deaminase.

Authors:  K L Smiley; A J Berry; C H Suelter
Journal:  J Biol Chem       Date:  1967-05-25       Impact factor: 5.157

9.  Modification by liposomes of the adenosine triphosphate-activating effect on adenylate deaminase from pig heart.

Authors:  J Purzycka-Preis; E Prus; M Woźniak; M Zydowo
Journal:  Biochem J       Date:  1978-11-01       Impact factor: 3.857

10.  In situ studies on AMP deaminase as a control system of the adenylate energy charge in yeasts.

Authors:  M Yoshino; K Murakami
Journal:  Biochim Biophys Acta       Date:  1981-01-07
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  1 in total

Review 1.  Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme.

Authors:  Francesca Ronca; Antonio Raggi
Journal:  Biomolecules       Date:  2018-08-23
  1 in total

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