Abstract
An acid lipase has been detected in bovine thyroid tissue using triolein as a substrate. The activity, probably associated with the lysosomes, displays a rather broad pH-optimum in the pH 4 to pH 6.5 range. The lipase activity can be partially purified by cosedimentation with lysosomes followed by solubilization through detergent and chromatography on Sephadex G-200 and carboxymethyl cellulose. The elution profile on Sephadex G-200 shows one peak (moleculare weight 67,000±2,000). In the final CM-cellulose step, two lipase peaks (lipase LA and lipase LB) are found. Sulhydryl reagents (iodoacetate, iodoacetamide, and N-ethylmaleimide) as well as mercuric ions markedly reduce both enzyme activities. Calcium ions, EDTA, and heparin have no effect. Sodium fluoride and diisopropylfluorophosphate are only slightly inhibitory. Sodium chloride causes a slight increase in both lipase activities. Anionic phospholipids such as cardiolipin and phosphatidylserine are not essential for enzyme activity.
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De Wolf, M., Lagrou, A., Hilderson, H.J. et al. Acid triacylglycerol lipase from bovine thyroid gland. Lipids 13, 598–604 (1978). https://doi.org/10.1007/BF02535822
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DOI: https://doi.org/10.1007/BF02535822