Some properties of triacylglycerol lipase in chicken erythrocytes

Membrane-bound acid lipase was found in the chicken erythrocytes ghosts, having an optimum pH of 4.5. The membrane-bound lipase showed its maximum activity at 38 degrees C, and it was stable below 45 degrees C. The bound lipase was activated by octyl glucoside and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), but it was markedly inhibited by chicken serum. The lipase was solubilized with CHAPS, but the solubilized lipase was labile. The solubilized lipase showed its maximum activity at pH 4.5, 38 degrees C, and it was stable below 40 degrees C. The solubilized lipase was activated by CHAPS and octyl glucoside. The lipase was markedly inhibited by chicken serum. The solubilized lipase have a molecular mass more than 230,000 by Sephacryl S-300 gel filtration.