Premium
Acyl‐CoA acyl‐sn glycerol‐3 phosphorylcholine acyl transferase of bovine mammary tissue
Author(s) -
Kinsella J. E.,
Infante J. P.
Publication year - 1974
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532140
Subject(s) - oleyl alcohol , phosphorylcholine , chemistry , glycerol , transferase , substrate (aquarium) , chromatography , glyceride , lipidology , microsome , acyl coa , biochemistry , clinical chemistry , enzyme , fatty acid , biology , oleic acid , ecology
Microsomal material from lactating bovine mammary tissue possess very active acyl‐CoA:1‐acyl‐sn‐glycerol‐3‐phosphorylcholine acyl transferase (EC2.3.1.‐1). Oleyl‐CoA was the preferred substrate and rates of 6.3, 6.4, 1.8, 21.0, and 0.1 nmoles acylated/min/mg were obtained for myristyl‐, palmityl‐, stearyl‐, oleyl‐ and linoleyl‐CoA, respectively, when 1‐oleyl‐sn‐glycerol‐3‐phosphorycholine was used compared to 5.2, 4.1, 1.0, 3.5, and 0.2 nmoles/min/mg with 1‐palmityl‐sn‐glycerol‐3‐phosphorylcholine as acyl acceptor. Apparent Km values of 4.5 and 5.2 μM for oleyl‐CoA and 6.5 and 4.6 μM for palmityl‐CoA were obtained with 1‐oleyl‐ and 1‐palmityl‐sn‐glycerol‐3‐phosphorylcholine, respectively. The Km values of 1‐oleyl‐sn‐glycerol‐3‐phosphorylcholine were 20 and 50 μM using oleyl‐CoA and palmityl‐CoA as acyl donors. The possible involvement of this enzyme in membrane dynamics during lipid secretion is discussed.