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Biophysical Journal 73: 230-238 (1997)
© 1997 the Biophysical Society

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Zero-order interfacial enzymatic degradation of phospholipid tubules.

P A Carlson, M H Gelb and P Yager

Department of Bioengineering, University of Washington, Seattle 98195, USA.

ABSTRACT

The first study of enzymatic hydrolysis of phospholipid tubules is reported. Phosphatidylcholines with acyl chains containing diacetylene groups are known to form tubular microstructures in which the lipids are tightly packed and crystalline. These tubules can be used to probe the role of microstructural form in the mechanics of interfacial enzymatic degradation by such enzymes as phospholipase A2 (PLA2). Hydrolysis by PLA2 may occur most rapidly in regions having the greatest number of bilayer packing defects, such as those that must be found at tubule ends. A microstructure that degrades primarily from its ends should exhibit zero-order kinetics, because the area of the degrading tubule and remains constant as the length of the microstructure decreases. Free fatty acid concentration was measured to follow the generation of PLA2 hydrolysis products in suspensions of diacetylenic phospholipid tubules. The kinetics of tubule hydrolysis were essentially zero-order until conversion was complete, as predicted. However, microscopy of partially hydrolyzed tubules revealed the formation of multiple discrete anionic product domains along the length of degrading tubules as well as in insoluble reaction product microstructures. Furthermore, the rate of tubule hydrolysis was only moderately enhanced by increasing the number of tubule ends, which is consistent with the conclusion that tubule ends are not the only sites of hydrolysis. A model that reconciles the overall kinetics with the morphological evidence is proposed.






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Copyright © 1997 by the Biophysical Society.