Abstract：
:Porcine pancreatic phospholipase A2 interacts with micelles of the substrate analogue n-octadecylphosphocholine to form a specific complex over considerably wide concentration ranges of both lipid and protein. UV absorption difference spectroscopy measurements indicate that the ratio of lipid to protein molecules in the complex is approximately 50. This number is confirmed by using other techniques to study the composition of the complex, namely, ultracentrifugation experiments and light scattering. The latter techniques furthermore demonstrate that the lipid--protein complex consists of 100 lipid and 2 enzyme molecules. Thus, the number of lipid molecules in the free micelle (200) is halved when the complex with phospholipase is being formed. The consequences of the results are discussed in relation to a theoretical model of the lipid--protein interaction.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Hille JD,Donné-Op den Kelder GM,Sauve P,de Haas GH,Egmond MRdoi
10.1021/bi00517a019subject
Has Abstractpub_date
1981-07-07 00:00:00pages
4068-73issue
14eissn
0006-2960issn
1520-4995journal_volume
20pub_type
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