Stearyl CoA as a precursor of oleic acid and glycerolipids in mammary microsomes from lactating bovine: Possible regulatory step in milk triglyceride synthesis

The stearyl desaturase of lactating bovine mammary tissue is located in the microsomes and requires activated fatty acid and NADH for activity. Other enzymes, acyl‐transferase(s) and deacylase which apparently compete with the desaturase for substrate are also present. Both the substrate 1‐14C‐stearyl CoA and the oleic acid produced by desaturase are esterified into the various lipid classes. The oleic acid is preferentially acylated into positionsn‐3 of the triglycerides andsn‐2 of the phosphatidylcholine. Experimental conditions causing reduced desaturase activity depressed triglyceride synthesis, and stimulation of desaturation by NADH L−α GP, acidic pH, 5.6, was accompanied by increased incorporation of radioactive fatty acids into the triglycerides. These data indicated that desaturase and glyceride acyl transferase were located contiguously within the microsomal membranes. The possibility that desaturase activity might control triglyceride synthesis in vivo is discussed. It was observed that mammary tissue from nonlactating cows 1–2 weeks and 2 days prior to calving lacked or possessed very low stearyl desaturase activity.