Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF.
Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF.
复制标题
人血清、滑液和脑脊液中组织蛋白酶 B、H 和 T 的低分子量抑制剂。
DOI：
10.1016/s0006-291x(82)80088-0
复制
发表时间：
1982
影响因子：
3.1
通讯作者：
Paul W.H. Chan
中科院分区：
文献类型：
--
作者：
J. Lenney;John Rose Liao;S. Sugg;Vijaya Gopalakrishnan;Henry C.H. Wong;Keith H. Ouye;Paul W.H. Chan
当人血浆在Sephadex G-75柱层析时，洗脱出相对分子质量为80,000和13,000的组织蛋白酶B抑制剂。高分子量峰(TpI-H)含有α-硫醇蛋白酶抑制剂和结合珠蛋白，两者都抑制组织蛋白B和H；低分子量峰(TpI-L)抑制组织蛋白B、H和T，但对木瓜酶、无花果酶和菠萝蛋白酶几乎没有或几乎没有活性。来自血浆的TPI-L含有两种分子形式的抑制物，而来自混合血清样本的TPI-L含有九种分子形式的抑制剂。血清TPI-L被发现不同于肺和许多其他器官中存在的低分子抑制物。用凝胶过滤分析类风湿滑液时，洗脱液中含有TPI-H和TPI-L。人脑脊液洗脱液中含有TPI-L，但不含TPI-H。
When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H.
支气管肺灌洗液中的蛋白水解酶：组织蛋白酶 B 样活性和脯氨酰内肽酶。
DOI：
--
发表时间：
1981
期刊：
The Journal of laboratory and clinical medicine
影响因子：
--
作者：
Orlowski,M;Orlowski,J;Lesser,M;Kilburn,KH
通讯作者：
Kilburn,KH