Purification and some characteristics of two human serum proteins inhibiting papain and other thiol proteinases
Purification and some characteristics of two human serum proteins inhibiting papain and other thiol proteinases
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两种抑制木瓜蛋白酶和其他硫醇蛋白酶的人血清蛋白的纯化及一些特性
DOI:
10.1016/0014-5793(79)80588-8
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发表时间:
1979
期刊:
影响因子:
3.5
通讯作者:
M. Järvinen
中科院分区:
文献类型:
--
作者:
M. Järvinen
Human serum contains 7 well characterized proteinase inhibitors with more or less broad specificity to serine proteinases [1, 2]. In addition, two inhibitors not inhibiting serine proteinases have been described: fl,-collagenase inhibitor [3] and cYz-thiol proteinase inhibitor [4]. The partially purified cuz-thiol proteinase inhibitor has been shown not to be identical with the known inhibitors of serine proteinases. Its properties are also quite different from those of the human epidermal thiol proteinase inhibitor, purified in our laboratory [5, 6].Here I describe the purification of two thiol proteinase inhibitors with (ILL-and CQ-mobilities from human serum. The purified inhibitors resemble each other in their immunological properties and inhibiting spectra, but have different charges and molecular sizes. The inhibitor with cYz-mobility seems to be identical with the thiol proteinase inhibitor in [4]. A preliminary note of this work has been published [7].