Comparison of properties of thiol proteinase inhibitors from rat serum and liver.
Comparison of properties of thiol proteinase inhibitors from rat serum and liver.
复制标题
大鼠血清和肝脏的硫醇蛋白酶抑制剂的特性比较。
DOI：
10.1016/s0021-9258(18)33331-3
复制
发表时间：
1982
期刊：
影响因子：
--
通讯作者：
N. Katunuma
中科院分区：
文献类型：
--
作者：
N. Wakamatsu;E. Kominami;N. Katunuma
对大鼠血清中的硫醇蛋白水解酶抑制物进行纯化，并与大鼠肝组织中的硫醇蛋白水解酶抑制物进行比较。用线性梯度洗脱的方法将大鼠血清中的抑制物分离为S-1、S-2和S-3三种形式。通过无花果凝胶层析柱和Sephadex G-150柱层析，得到一种纯的抑制物(S1)。S_1、S_2和S_3在Sephadex G-150柱上的表观分子量分别为90,000，95,000和160,000。血清硫醇蛋白水解酶抑制物和肝脏硫醇蛋白水解酶的不同之处在于：1)三种形式的血清抑制物的相对分子质量均明显高于肝脏硫醇蛋白水解酶抑制物(Mr=12,500)；2)血清抑制物和肝抑制物在抗血清或抗肝抗血清中均无交叉反应；3)血清抑制物和肝抑制物对硫醇蛋白水解酶具有特异性，但具有不同的抑制谱；4)肝抑制物不与刀豆蛋白A-琼脂糖凝胶结合，而血清抑制物与α-甲基甘露糖苷结合并洗脱。在组织匀浆中检测到一种高相对分子质量的硫醇蛋白酶抑制剂，它显著抑制木瓜酶，但不抑制组织蛋白酶H。灌流器官使其活性降低，表明它来自血清。
Thiol proteinase inhibitors in rat serum were purified and their properties were compared with those of rat liver thiol proteinase inhibitor. The inhibitors in rat serum were separated into three forms (S-1, S-2, and S-3) by linear gradient elution from a DE52 column. One inhibitor (S1) was purified to homogeneity by chromatography on ficin-bound Sepharose and Sephadex G-150 columns. The apparent molecular weights of S1, S2, and S3 on Sephadex G-150 columns were 90,000, 95,000, and 160,000, respectively. Serum thiol proteinase inhibitor and liver thiol proteinase differed in the following: 1) all three forms of serum inhibitor had much higher molecular weights than the liver thiol proteinase inhibitor (Mr = 12,500); 2) no cross-reactivity was observed between serum inhibitors and liver inhibitor in tests with either antiserum inhibitor or anti-liver antiserum; 3) both serum inhibitor and liver inhibitor were specific for thiol proteinases, but had different inhibition spectra; 4) the liver inhibitor did not bind to concanavalin A-Sepharose, whereas the serum inhibitor bound and was eluted with alpha-methyl mannoside. A thiol proteinase inhibitor of high molecular weight detected in tissue homogenates inhibited papain markedly but did not inhibit cathepsin H. Its activity was diminished by perfusion of the organ, indicating that it is derived from serum.