7330

Biochemistry 1991, 30, 7330-7340

Interfacial Catalysis by Phospholipase A2: Monomeric Enzyme Is Fully Catalytically Active at the Bilayer Interface? Mahendra Kumar Jain,*.* Girish Ranadive,* Bao-Zhu Yu,* and H. M. Verheijs Department of Chemistry, University of Delaware, Newark, Delaware 19716, and Department of Biochemistry, State University, Utrecht, The Netherlands Received September 17, 1990; Revised Manuscript Received March 26, 1991

Interfacial catalysis in the scooting mode by phospholipase A2 (PLA2) from pancreas and venoms ( 18 different preparations) was examined on vesicles of 1,2-dimyristoyl-sn-glycero-3-phosphomethanolunder the conditions where the rates of transbilayer and intervesicle exchanges of the enzyme, substrate, and the products of hydrolysis were negligible on the time scale (

Interfacial catalysis by phospholipase A2: monomeric enzyme is fully catalytically active at the bilayer interface.

Interfacial catalysis in the scooting mode by phospholipase A2 (PLA2) from pancreas and venoms (18 different preparations) was examined on vesicles of...
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