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Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data.

作者信息

Müller-Esterl W, Fritz H, Machleidt W, Ritonja A, Brzin J, Kotnik M, Turk V, Kellermann J, Lottspeich F

出版信息

FEBS Lett. 1985 Mar 25;182(2):310-4. doi: 10.1016/0014-5793(85)80322-7.

DOI:10.1016/0014-5793(85)80322-7
PMID:2579850
Abstract

Human high- and low-Mr kininogens were shown to be potent inhibitors of cysteine proteinases such as cathepsin L and papain (Ki = 17-48 pM). A strong immunological cross-reaction between the kininogens and low-Mr alpha-cysteine proteinase inhibitor from human plasma was found. Comparison of partial amino acid sequences from high- and low-Mr kininogen and low-Mr alpha-cysteine proteinase inhibitor demonstrated sequence identity for all segments analyzed. These findings suggest that the kininogens and the alpha-cysteine proteinase inhibitors from human plasma are identical proteins.

摘要

相似文献

1
Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data.
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2
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The role of the kininogens as cysteine proteinase inhibitors in local and systemic inflammation.激肽原作为半胱氨酸蛋白酶抑制剂在局部和全身炎症中的作用。
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Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.鸡半胱氨酸蛋白酶抑制剂与人类激肽原结构域2序列的杂合体对钙蛋白酶表现出新型抑制作用,对肌动蛋白酶的抑制作用增强,而对木瓜蛋白酶、组织蛋白酶L和组织蛋白酶B的抑制作用受损。
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Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.
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Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments.
Eur J Biochem. 1988 Apr 5;173(1):185-90. doi: 10.1111/j.1432-1033.1988.tb13983.x.

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