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    Chapter

    Regulation of Pancreatic Phospholipase A2 Activity by Different Lipid-Water Interfaces

    Pancreatic phospholipase A2 interacts with lipid-water interfaces by means of a specific region, the Interface Recognition Site (IRS), which most probably penetrates to a certain extent into the hydrophobic inter...

    M. C. E. van Dam-Mieras, A. J. Slotboom, H. M. Verheij in Structure of Biological Membranes (1977)

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    Chapter

    Relationship between Structure and Activity of Pancreatic Phospholipase A2

    Phospholipase A2 (EC 3.1.1.4) hydrolyzes exclusively the 2­acyl ester linkage of all types of naturally occurring phosphogly­cerides (1). The enzyme acts highly stereospecific and only 3-sn­phosphoglycerides are ...

    A. J. Slotboom, M. C. E. van Dam-Mieras, E. H. J. M. Jansen in Enzymes of Lipid Metabolism (1978)

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    Chapter

    Phospholipase A2 Interaction with Various Phospholipids. A Model for the Lipoprotein Molecule?

    This NATO-workshop is devoted to the structure and function of the lipoprotein molecule. Important building stones of these complexes are the so-called“apoproteins” and phospholipids. Considerable progress has...

    G. H. de Haas, A. J. Slotboom, H. M. Verheij, J. C. Vidal in The Lipoprotein Molecule (1978)

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    Chapter

    Studies of Lipase and Phospholipase A2 Acting on Lipid Monolayers

    Le phénomène de la pénétration dans des films lipidiques mono-moléculaires de différents enzymes lipolytiques a été étudié grâce à la méthode du barostat superficiel. Le temps d’induction, mesuré durant l’état...

    R. Verger, J. Rietsch, F. Pattus, F. Ferrato, G. Pieroni in Enzymes of Lipid Metabolism (1978)

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    Article

    Does a chemically symmetric bond pattern induce a symmetric conformation of lecithin molecules in membranes?

    G. Büldt, G. H. de Haas, J. Seelig in Biophysics of structure and mechanism (1980)

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    Chapter

    Structure and function of phospholiphase A2

    H. M. Verheij, A. J. Slotboom, G. H. de Haas in Reviews of Physiology, Biochemistry and Ph… (1981)

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    Chapter

    The Interaction of Pancreatic Phospholipase A2 with Negatively Charged Substrates — Application: The Transformation of Soluble Phospholipase A2 into a Highly Penetrating “Membrane-Bound” Form

    This study deals with some kinetic properties of porcine pancreatic phospholipase A2 (PLA2) acting on neutral and anionic substrates. Short—chain diacylglycerosulfates possess a much higher affinity to the enzyme...

    G. H. de Haas, A. J. Slotboom, M. G. van Oort in Enzymes of Lipid Metabolism II (1986)

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    Chapter

    Probing the Mechanism of Pancreatic Phospholipase A2 with the Aid of Recombinant DNA Techniques

    Phospholipase A2 (E.C. 3.1.1.4) attacks the acyl ester bond at position 2 of 3-sn-phosphoglycerides (van Deenen en de Haas, 1963). The in-vivo importance of phospholipase A2 (PLA) is reflected by the fact that th...

    O. P. Kuipers, C. J. van den Bergh in Biochemistry, Molecular Biology, and Physi… (1990)

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    Article

    Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor

    The three-dimensional structure of porcine pancreatic PLA2 (PLA2), present in a 40 kDa ternary complex with micelles and a competitive inhibitor, has been determined using multidimensional heteronuclear NMR spect...

    B. van den Berg, M. Tessari, R. Boelens, R. Dijkman in Journal of Biomolecular NMR (1995)