Lanzillo J J, Fanburg B L
Biochim Biophys Acta. 1977 Mar 28;491(1):339-44. doi: 10.1016/0005-2795(77)90071-x.
A low molecular weight angiotensin I converting enzyme (light angiotensin enzyme) was isolated from a homogenate of rat lung subjected to dialysis against sodium acetate at pH 4.8. This enzyme has a molecular weight of 84 000 on Sephadex G-200 and a molecular weight of 91 000 on SDS-poly-acrylamide gel as compared with a molecular weight of 139 000 for angiotensin I converting enzyme on SDS-polyacrylamide. Light angiotensin enzyme was activated by NaCl and inhibited by EDTA, angiotensin II, and bradykinin potentiating factor nonapeptide. Light angiotensin enzyme cross-reacted with antibody prepared against angiotensin I converting enzyme and stained with periodic acid-Schiff reagent as a glycoprotein. The evidence suggests that light angiotensin enzyme is a fragment of the higher molecular weight enzyme.
从经pH 4.8的醋酸钠透析的大鼠肺匀浆中分离出一种低分子量血管紧张素I转换酶(轻血管紧张素酶)。与SDS-聚丙烯酰胺凝胶上分子量为139000的血管紧张素I转换酶相比,该酶在Sephadex G-200上的分子量为84000,在SDS-聚丙烯酰胺凝胶上的分子量为91000。轻血管紧张素酶被NaCl激活,被EDTA、血管紧张素II和缓激肽增强因子九肽抑制。轻血管紧张素酶与针对血管紧张素I转换酶制备的抗体发生交叉反应,并用高碘酸-希夫试剂染色,显示为一种糖蛋白。证据表明,轻血管紧张素酶是高分子量酶的一个片段。