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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...
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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 ...
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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...
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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...
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Article
Does a chemically symmetric bond pattern induce a symmetric conformation of lecithin molecules in membranes?
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Chapter
Structure and function of phospholiphase A2
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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...
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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...
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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...