Okabe T, Yorifuji H, Murase T, Takaku F
Biochem Biophys Res Commun. 1984 Nov 30;125(1):273-8. doi: 10.1016/s0006-291x(84)80364-2.
The lipase released by heparin infusion into perfused rat lungs is shown to be identical with lipoprotein lipase on the basis of the following characteristics: 1) it required plasma for full activity; 2) it was largely inhibited by 1 M NaCl; and 3) it bound to a heparin-Sepharose gel and eluted with buffer containing 1.5 M NaCl. Macrophages prepared from rat lungs released a considerable amount of lipoprotein lipase, with characteristics similar to those of the lipoprotein lipase released from heparin-perfused rat lungs. Pulmonary surfactant-producing type II pneumocytes did not cause a significant release of lipoprotein lipase. No apparent lipoprotein lipase activities were detected in the conditioned medium of other lung cells from which macrophages had been selectively removed.
基于以下特征,经肝素注入灌注大鼠肺脏所释放的脂肪酶被证明与脂蛋白脂肪酶相同:1)它需要血浆才能发挥全部活性;2)它在很大程度上受到1M氯化钠的抑制;3)它与肝素-琼脂糖凝胶结合,并在含有1.5M氯化钠的缓冲液中洗脱。从大鼠肺脏制备的巨噬细胞释放出大量脂蛋白脂肪酶,其特征与从肝素灌注大鼠肺脏释放的脂蛋白脂肪酶相似。产生肺表面活性物质的II型肺上皮细胞不会导致脂蛋白脂肪酶的显著释放。在已选择性去除巨噬细胞的其他肺细胞的条件培养基中未检测到明显的脂蛋白脂肪酶活性。