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Photolabeling acyl CoA binding proteins in microsome preparations
Author(s) -
Hare James F
Publication year - 1995
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(95)01177-g
Subject(s) - microsome , biochemistry , chemistry , enzyme , coenzyme a , diacylglycerol kinase , acyltransferases , membrane protein , acylation , acyl coa , membrane , biosynthesis , protein kinase c , reductase , catalysis
To identify key enzymes that participate in acylglycerol metabolism, 12‐[(5‐iodo‐4‐azidosalicyl)amino]dodecanoylcoenzyme A (ASACoA) was emploued as a photoaffinity label for those enzymes that use fatty acyl CoA as a co‐substrate. ASACoA inhibited diacylglycerol acyltransferase activity in liver microsomes and was incorporated into triacylglycerol in a microsome dependent reaction. When photoactivated, ASACoA labeled four proteins in rat liver (75, 54, 50 and 37 kDa) and in epididymal fat cell (75, 64, 54 and 37 kDa) microsomes. Photolabeling was sensitive to palmitoyl CoA. After solubilization in Triton X‐114, all four proteins were concentrated into the detergent phase, indicating that they are integral membrane proteins.