Fujii M, Nishisako S, Fukunaga T, Koga K
Int J Biochem. 1986;18(4):395-8. doi: 10.1016/0020-711x(86)90047-9.
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.
在鸡红细胞血影中发现了膜结合酸性脂肪酶，其最适pH值为4.5。膜结合脂肪酶在38℃时表现出最大活性，在45℃以下稳定。结合脂肪酶可被辛基葡糖苷和3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐（CHAPS）激活，但受到鸡血清的显著抑制。脂肪酶用CHAPS溶解，但溶解后的脂肪酶不稳定。溶解后的脂肪酶在pH 4.5、38℃时表现出最大活性，在40℃以下稳定。溶解后的脂肪酶可被CHAPS和辛基葡糖苷激活。该脂肪酶受到鸡血清的显著抑制。通过Sephacryl S-300凝胶过滤，溶解后的脂肪酶分子量超过230,000。
