人体关节软骨提取物含有组织金属蛋白酶抑制剂。
Extracts of human articular cartilage contain an inhibitor of tissue metalloproteinases.
作者信息
Dean D D, Woessner J F
出版信息
Biochem J. 1984 Feb 15;218(1):277-80. doi: 10.1042/bj2180277.
Abstract
When human articular cartilage is extracted with 2M-guanidinium hydrochloride at pH 7.5, an inhibitor is obtained that blocks the activity of three metalloproteinases, including collagenase. Molecular-sieve chromatography of the inhibitor gives an Mr value for the inhibitor of 28 500. The inhibitor is stable to heat (60 degrees C, 1h) and acid (pH2, 24 degrees C, 10 min). It is destroyed by trypsin and by reduction and alkylation. It is slowly inactivated by aminophenylmercuric acetate. It binds to concanavalin A-Sepharose and is eluted with alpha-D-1-O-methyl glucopyranoside. Complexes of enzyme and inhibitor are not re-activated by aminophenylmercuric acetate and only partially so by high levels of trypsin. These properties indicate that this inhibitor is a member of the TIMP (tissue inhibitor of metalloproteinases) class. Such an inhibitor, previously found in tissue culture and amniotic fluid, is now shown to be directly extractable from tissue.
摘要
当在pH 7.5条件下用2M盐酸胍提取人关节软骨时，可获得一种抑制剂，它能抑制包括胶原酶在内的三种金属蛋白酶的活性。该抑制剂经分子筛层析测得其相对分子质量为28500。该抑制剂对热（60℃，1小时）和酸（pH2，24℃，10分钟）稳定。它可被胰蛋白酶以及还原和烷基化作用破坏。它会被氨基苯基汞乙酸盐缓慢灭活。它能与伴刀豆球蛋白A - 琼脂糖结合，并用α - D - 1 - O - 甲基吡喃葡萄糖苷洗脱。酶与抑制剂的复合物不会被氨基苯基汞乙酸盐重新激活，只有在高浓度胰蛋白酶作用下才会部分重新激活。这些特性表明该抑制剂是金属蛋白酶组织抑制剂（TIMP）家族的一员。这种先前在组织培养物和羊水中发现的抑制剂，现在表明可直接从组织中提取。
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