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Utilization of membranous lipid substrates by membrane‐bound enzymes
Author(s) -
Rousseau A.,
Gatt S.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80829-7
Subject(s) - microsome , phospholipase , enzyme , diacylglycerol kinase , substrate (aquarium) , biochemistry , membrane , chemistry , lipase , hydrolysis , phospholipase c , biology , ecology , protein kinase c
The membranous lipase of rat liver microsomes was used to hydrolyze diacylglycerol (DG), generated within the microsomal membrane by treatment with phospholipase C, in two separate interactions. For an intramembrane enzyme‐substrate interaction, the enzyme and DG were present in the same microsomes. For intermembrane interactions, native microsomes of rat liver were used as carriers of the enzyme, while heated and phospholipase C‐treated microsomes of rat liver or brain were employed as carriers of the substrate. The v vs S curves of the intermembrane interaction were hyperbolic while those of the intramembrane utilization were parabolic.