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从牛主动脉培养物中提取的胶原酶抑制剂的纯化及特性

Purification and properties of a collagenase inhibitor from cultures of bovine aorta.

作者信息

Nolan J C, Ridge S C, Oronsky A L, Kerwar S S

出版信息

Atherosclerosis. 1980 Jan;35(1):93-102. doi: 10.1016/0021-9150(80)90031-3.

DOI:10.1016/0021-9150(80)90031-3
PMID:6245663
Abstract

Bovine medial explants in culture synthesize a potent inhibitor of mammalian collagenase but not of bacterial collagenase. This inhibitor has been partially purified and has an apparent molecular weight of 45,000. It is a glycoprotein and is stable to heat, trypsin, acid and mercurials. Inhibitory activity is destroyed on reductive alkylation. The inhibitor interacts with collagenase and this interaction leads to the loss of enzymatic activity. This inhibitor may play a physiological role in the control of collagen degradation in blood vessels.

摘要

培养中的牛内侧外植体可合成一种有效的哺乳动物胶原酶抑制剂,但不能合成细菌胶原酶抑制剂。这种抑制剂已被部分纯化,其表观分子量为45,000。它是一种糖蛋白,对热、胰蛋白酶、酸和汞稳定。还原烷基化会破坏其抑制活性。该抑制剂与胶原酶相互作用,这种相互作用会导致酶活性丧失。这种抑制剂可能在控制血管中胶原降解方面发挥生理作用。

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Purification and properties of a collagenase inhibitor from cultures of bovine aorta.从牛主动脉培养物中提取的胶原酶抑制剂的纯化及特性
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引用本文的文献

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MMPs and TIMPs--an historical perspective.基质金属蛋白酶与基质金属蛋白酶组织抑制因子——历史视角
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Extracts of human articular cartilage contain an inhibitor of tissue metalloproteinases.人体关节软骨提取物含有组织金属蛋白酶抑制剂。
Biochem J. 1984 Feb 15;218(1):277-80. doi: 10.1042/bj2180277.
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The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor.纯化的兔骨胶原酶与纯化的兔骨金属蛋白酶抑制剂之间的相互作用。
Biochem J. 1983 May 1;211(2):313-8. doi: 10.1042/bj2110313.
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Purification of rabbit bone inhibitor of collagenase.兔骨胶原酶抑制剂的纯化
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